T00043
type: Enzyme
active site residues resources: Identification of tyrosine and lysine peptides labeled by 5'-p-fluorosulfonylbenzoyl adenosine in the active site of pyruvate kinase.
active site residues resources: The monovalent cation requirement of rabbit muscle pyruvate kinase is eliminated by substitution of lysine for glutamate 117.
active site residues resources: Conformational changes in yeast pyruvate kinase studied by 205Tl+ NMR.
cath: Pyruvate Kinase; Chain
cath: TIM Barrel
cath: M1 Pyruvate Kinase; Domain 3
csa: 1pkn
ec: https://purl.uniprot.org/enzyme/2.7.1.40
kegg cofactor: Magnesium
kegg cofactor: Potassium
kegg enzyme: pyruvate kinase
kegg pathway: Glycolysis / Gluconeogenesis
kegg pathway: Purine metabolism
kegg pathway: Pyruvate metabolism
kegg pathway: Carbon fixation in photosynthetic organisms
kegg product: ATP
kegg product: Pyruvate
kegg substrate: ADP
kegg substrate: Phosphoenolpyruvate
macie: M0326
pdb: 1e0tA01
pdb: 1e0tB01
pdb: 1e0tC01
pdb: 1e0tD01
pdb: 1e0uA01
pdb: 1e0uB01
pdb: 1e0uC01
pdb: 1e0uD01
pdb: 1pkyA01
pdb: 1pkyB01
pdb: 1pkyC01
pdb: 1pkyD01
pdb: 1a3wA01
pdb: 1a3wB01
pdb: 1a3xA01
pdb: 1a3xB01
pdb: 1pklA01
pdb: 1pklB01
pdb: 1pklC01
pdb: 1pklD01
pdb: 1pklE01
pdb: 1pklF01
pdb: 1pklG01
pdb: 1pklH01
pdb: 1a49A01
pdb: 1a49B01
pdb: 1a49C01
pdb: 1a49D01
pdb: 1a49E01
pdb: 1a49F01
pdb: 1a49G01
pdb: 1a49H01
pdb: 1a5uA01
pdb: 1a5uB01
pdb: 1a5uC01
pdb: 1a5uD01
pdb: 1a5uE01
pdb: 1a5uF01
pdb: 1a5uG01
pdb: 1a5uH01
pdb: 1aqfA01
pdb: 1aqfB01
pdb: 1aqfC01
pdb: 1aqfD01
pdb: 1aqfE01
pdb: 1aqfF01
pdb: 1aqfG01
pdb: 1aqfH01
pdb: 1f3wA01
pdb: 1f3wB01
pdb: 1f3wC01
pdb: 1f3wD01
pdb: 1f3wE01
pdb: 1f3wF01
pdb: 1f3wG01
pdb: 1f3wH01
pdb: 1f3xA01
pdb: 1f3xB01
pdb: 1f3xC01

Analogue
compound: Phosphoenolpyruvate
ligand het code: PGA
pdb: 1a3wA02

Analogue
compound: Phosphoenolpyruvate
ligand het code: PGA
pdb: 1a3wB02

Analogue
compound: Phosphoenolpyruvate
ligand het code: PGA
pdb: 1a3xA02

Analogue
compound: Phosphoenolpyruvate
ligand het code: PGA
pdb: 1a3xB02

Analogue
compound: Phosphoenolpyruvate
ligand het code: PGA
pdb: 1liuA02

Analogue
compound: Phosphoenolpyruvate
ligand het code: PGA
pdb: 1liuB02

Analogue
compound: Phosphoenolpyruvate
ligand het code: PGA
pdb: 1liuC02

Analogue
compound: Phosphoenolpyruvate
ligand het code: PGA
pdb: 1liuD02

Analogue
compound: Phosphoenolpyruvate
ligand het code: PGA
pdb: 1liwA02

Analogue
compound: Phosphoenolpyruvate
ligand het code: PGA
pdb: 1liwB02

Analogue
compound: Phosphoenolpyruvate
ligand het code: PGA
pdb: 1liwC02

Analogue
compound: Phosphoenolpyruvate
ligand het code: PGA
pdb: 1liwD02

Analogue
compound: Phosphoenolpyruvate
ligand het code: PGA
pdb: 1lixA02

Analogue
compound: Phosphoenolpyruvate
ligand het code: PGA
pdb: 1lixB02

Analogue
compound: Phosphoenolpyruvate
ligand het code: PGA
pdb: 1lixC02

Analogue
compound: Phosphoenolpyruvate
ligand het code: PGA
pdb: 1lixD02

Analogue
compound: Phosphoenolpyruvate
ligand het code: PGA
pdb: 1liyA02

Analogue
compound: Phosphoenolpyruvate
ligand het code: PGA
pdb: 1liyB02

Analogue
compound: Phosphoenolpyruvate
ligand het code: PGA
pdb: 1liyC02

Analogue
compound: Phosphoenolpyruvate
ligand het code: PGA
pdb: 1liyD02

Analogue
compound: Magnesium
ligand het code: _MN
pdb: 1a3wA02

Analogue
compound: Magnesium
ligand het code: _MN
pdb: 1a3wB02

Analogue
compound: Magnesium
ligand het code: _MN
pdb: 1a3xA02

Analogue
compound: Magnesium
ligand het code: _MN
pdb: 1a3xB02

Analogue
compound: Magnesium
ligand het code: _MN
pdb: 1f3wA02

Analogue
compound: Magnesium
ligand het code: _MN
pdb: 1f3wB02

Analogue
compound: Magnesium
ligand het code: _MN
pdb: 1f3wC02

Analogue
compound: Magnesium
ligand het code: _MN
pdb: 1f3wD02

Analogue
compound: Magnesium
ligand het code: _MN
pdb: 1f3wE02

Analogue
compound: Magnesium
ligand het code: _MN
pdb: 1f3wF02

Analogue
compound: Magnesium
ligand het code: _MN
pdb: 1f3wG02

Analogue
compound: Magnesium
ligand het code: _MN
pdb: 1f3wH02

Analogue
compound: Magnesium
ligand het code: _MN
pdb: 1f3xA02

Analogue
compound: Magnesium
ligand het code: _MN
pdb: 1f3xB02

Analogue
compound: Magnesium
ligand het code: _MN
pdb: 1f3xC02

Analogue
compound: Magnesium
ligand het code: _MN
pdb: 1f3xD02

Analogue
compound: Magnesium
ligand het code: _MN
pdb: 1f3xE02

Analogue
compound: Magnesium
ligand het code: _MN
pdb: 1f3xF02

Analogue
compound: Magnesium
ligand het code: _MN
pdb: 1f3xG02

Analogue
compound: Magnesium
ligand het code: _MN
pdb: 1f3xH02

Analogue
compound: Magnesium
ligand het code: _MN
pdb: 1pknA02

Analogue
compound: Magnesium
ligand het code: _MN
pdb: 1liuA02

Analogue
compound: Magnesium
ligand het code: _MN
pdb: 1liuB02

Analogue
compound: Magnesium
ligand het code: _MN
pdb: 1liuC02

Analogue
compound: Magnesium
ligand het code: _MN
pdb: 1liuD02

Analogue
compound: Magnesium
ligand het code: _MN
pdb: 1liwA02

Analogue
compound: Magnesium
ligand het code: _MN
pdb: 1liwB02

Analogue
compound: Magnesium
ligand het code: _MN
pdb: 1liwC02

Analogue
compound: Magnesium
ligand het code: _MN
pdb: 1liwD02

Analogue
compound: Magnesium
ligand het code: _MN
pdb: 1lixA02

Analogue
compound: Magnesium
ligand het code: _MN
pdb: 1lixB02

Analogue
compound: Magnesium
ligand het code: _MN
pdb: 1lixC02

Analogue
compound: Magnesium
ligand het code: _MN
pdb: 1lixD02

Analogue
compound: Magnesium
ligand het code: _MN
pdb: 1liyA02

Analogue
compound: Magnesium
ligand het code: _MN
pdb: 1liyB02

Analogue
compound: Magnesium
ligand het code: _MN
pdb: 1liyC02

Analogue
compound: Magnesium
ligand het code: _MN
pdb: 1liyD02

Analogue
compound: Potassium
ligand het code: _NA
pdb: 1a5uA02

Analogue
compound: Potassium
ligand het code: _NA
pdb: 1a5uB02

Analogue
compound: Potassium
ligand het code: _NA
pdb: 1a5uC02

Analogue
compound: Potassium
ligand het code: _NA
pdb: 1a5uD02

Analogue
compound: Potassium
ligand het code: _NA
pdb: 1a5uE02

Analogue
compound: Potassium
ligand het code: _NA
pdb: 1a5uF02

Analogue
compound: Potassium
ligand het code: _NA
pdb: 1a5uG02

Analogue
compound: Potassium
ligand het code: _NA
pdb: 1a5uH02

Analogue
compound: Pyruvate
ligand het code: OXL
pdb: 1a49A02

Analogue
compound: Pyruvate
ligand het code: OXL
pdb: 1a49B02

Analogue
compound: Pyruvate
ligand het code: OXL
pdb: 1a49C02

Analogue
compound: Pyruvate
ligand het code: OXL
pdb: 1a49D02

Analogue
compound: Pyruvate
ligand het code: OXL
pdb: 1a49E02

Analogue
compound: Pyruvate
ligand het code: OXL
pdb: 1a49F02

Analogue
compound: Pyruvate
ligand het code: OXL
pdb: 1a49G02

Analogue
compound: Pyruvate
ligand het code: OXL
pdb: 1a49H02

Analogue
compound: Pyruvate
ligand het code: OXL
pdb: 1a5uA02

Analogue
compound: Pyruvate
ligand het code: OXL
pdb: 1a5uB02

Analogue
compound: Pyruvate
ligand het code: OXL
pdb: 1a5uC02

Analogue
compound: Pyruvate
ligand het code: OXL
pdb: 1a5uD02

Analogue
compound: Pyruvate
ligand het code: OXL
pdb: 1a5uE02

Analogue
compound: Pyruvate
ligand het code: OXL
pdb: 1a5uF02

Analogue
compound: Pyruvate
ligand het code: OXL
pdb: 1a5uG02

Analogue
compound: Pyruvate
ligand het code: OXL
pdb: 1a5uH02

Analogue
compound: Pyruvate
ligand het code: OXL
pdb: 1t5aA02

Analogue
compound: Pyruvate
ligand het code: OXL
pdb: 1t5aB02

Analogue
compound: Pyruvate
ligand het code: OXL
pdb: 1t5aC02

Analogue
compound: Pyruvate
ligand het code: OXL
pdb: 1t5aD02

ReferenceForCatalyticMechanism
reference index: 1
reference section: Fig.4, Fig.12, p.204

ReferenceForCatalyticMechanism
reference index: 4
reference section: Fig.3, p.629

ReferenceForCatalyticMechanism
reference index: 8
reference section: Scheme II

ReferenceForCatalyticMechanism
reference index: 10
reference section: Fig.5, p.478-480

ReferenceForCatalyticMechanism
reference index: 13
reference section: Fig.7

ReferenceForCatalyticMechanism
reference index: 28
reference section: p.731-734, p.737

ReferenceForCatalyticMechanism
reference index: 33

ReferenceForCatalyticMechanism
reference index: 36
reference section: p.6253-6254

ReferenceForCatalyticMechanism
reference index: 39
reference section: p.201-204

ReferenceForCatalyticMechanism
reference index: 40
reference section: p.9142-9144

ReferenceForCatalyticMechanism
reference index: 41
reference section: p.623-624

ReferenceForCatalyticMechanism
reference index: 52

ReferenceForCatalyticMechanism
reference index: 53
reference section: Fig.1, p.9423-9424

M1 Pyruvate Kinase; Domain 3
type: Cath
catalytic domain: index.html
references: http://www.cathdb.info/version/latest/superfamily/2.40.33.10

TIM Barrel
type: Cath
catalytic domain: index.html
references: http://www.cathdb.info/version/latest/superfamily/3.20.20.60

Pyruvate Kinase; Chain
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.40.1380.20

Glycolysis / Gluconeogenesis
type: KeggPathway
references: KEGG:MAP00010

Purine metabolism
type: KeggPathway
references: KEGG:MAP00230

Pyruvate metabolism
type: KeggPathway
references: KEGG:MAP00620

Carbon fixation in photosynthetic organisms
type: KeggPathway
references: KEGG:MAP00710

Nuclear relaxation studies of the role of the divalent cation in the mechanism of pyruvate kinase and enolase: inner sphere and second sphere complexes.
type: BibliographicResource
authors:
  item: Mildvan AS
  item: Nowak T
  item: Fung CH
journal: Ann N Y Acad Sci
pages: 192-210
published year: 1973
volume: 222
references: http://www.ncbi.nlm.nih.gov/pubmed/4522427

The structure of cat muscle pyruvate kinase.
type: BibliographicResource
authors:
  item: Muirhead H
  item: Clayden DA
  item: Barford D
  item: Lorimer CG
  item: Fothergill-Gilmore LA
  item: Schiltz E
  item: Schmitt W
journal: EMBO J
pages: 475-81
published year: 1986
volume: 5
references: http://www.ncbi.nlm.nih.gov/pubmed/3519210

Crystallographic studies on the structure and catalytic activity of pyruvate kinase from skeletal muscle.
type: BibliographicResource
authors:
  item: Muirhead H
  item: Clayden DA
  item: Cuffe SP
  item: Davies C
journal: Biochem Soc Trans
pages: 996-9
published year: 1987
volume: 15
references: http://www.ncbi.nlm.nih.gov/pubmed/3691955

Structure of the oxalate-ATP complex with pyruvate kinase: ATP as a bridging ligand for the two divalent cations.
type: BibliographicResource
authors:
  item: Lodato DT
  item: Reed GH
journal: Biochemistry
pages: 2243-50
published year: 1987
volume: 26
references: http://www.ncbi.nlm.nih.gov/pubmed/3040085

Nuclear Overhauser effect studies of the conformations of MgATP bound to the active and secondary sites of muscle pyruvate kinase.
type: BibliographicResource
authors:
  item: Rosevear PR
  item: Fox TL
  item: Mildvan AS
journal: Biochemistry
pages: 3487-93
published year: 1987
volume: 26
references: http://www.ncbi.nlm.nih.gov/pubmed/3498511

Yeast pyruvate kinase: essential lysine residues in the active site.
type: BibliographicResource
authors:
  item: Imarai M
  item: Hinrichsen P
  item: Bazaes S
  item: Wilkens M
  item: Eyzaguirre J
journal: Int J Biochem
pages: 1001-8
published year: 1988
volume: 20
references: http://www.ncbi.nlm.nih.gov/pubmed/3143610

Domain interaction in rabbit muscle pyruvate kinase. II. Small angle neutron scattering and computer simulation.
type: BibliographicResource
authors:
  item: Consler TG
  item: Uberbacher EC
  item: Bunick GJ
  item: Liebman MN
  item: Lee JC
journal: J Biol Chem
pages: 2794-801
published year: 1988
volume: 263
references: http://www.ncbi.nlm.nih.gov/pubmed/3343233

Domain interaction in rabbit muscle pyruvate kinase. II. Small angle neutron scattering and computer simulation.
type: BibliographicResource
authors:
  item: Consler TG
  item: Uberbacher EC
  item: Bunick GJ
  item: Liebman MN
  item: Lee JC
journal: J Biol Chem
pages: 2794-801
published year: 1988
volume: 263
references: http://www.ncbi.nlm.nih.gov/pubmed/3343233

Crystal structure of enolase indicates that enolase and pyruvate kinase evolved from a common ancestor.
type: BibliographicResource
authors:
  item: Lebioda L
  item: Stec B
journal: Nature
pages: 683-6
published year: 1988
volume: 333
references: http://www.ncbi.nlm.nih.gov/pubmed/3374614

2-[(4-Bromo-2,3-dioxobutyl)thio]-1,N6-ethenoadenosine 5'-diphosphate. A new fluorescent affinity label of a tyrosyl residue in the active site of rabbit muscle pyruvate kinase.
type: BibliographicResource
authors:
  item: DeCamp DL
  item: Colman RF
journal: J Biol Chem
pages: 8430-41
published year: 1989
volume: 264
references: http://www.ncbi.nlm.nih.gov/pubmed/2489027

Three-dimensional structure of cat muscle pyruvate kinase at 6 Angstrom resolution.
type: BibliographicResource
authors:
  item: Stammers DK
  item: Muirhead H
journal: J Mol Biol
medline id: 76048760
pages: 213-25
published year: 1975
volume: 95
references: http://www.ncbi.nlm.nih.gov/pubmed/1185780
references: P11979
comment: X-RAY CRYSTALLOGRAPHY (6 ANGSTROMS)

Cysteinyl peptides of rabbit muscle pyruvate kinase labeled by the affinity label 8-[(4-bromo-2,3-dioxobutyl)thio]adenosine 5'-triphosphate.
type: BibliographicResource
authors:
  item: Vollmer SH
  item: Colman RF
journal: Biochemistry
pages: 2495-501
published year: 1990
volume: 29
references: http://www.ncbi.nlm.nih.gov/pubmed/2334678

Crystallization and preliminary analysis of enzyme-substrate complexes of pyruvate kinase from rabbit muscle.
type: BibliographicResource
authors:
  item: Schmidt-Base K
  item: Buchbinder JL
  item: Reed GH
  item: Rayment I
journal: Proteins
pages: 153-7
published year: 1991
volume: 11
references: http://www.ncbi.nlm.nih.gov/pubmed/1658780

The cooperative binding of fructose-1,6-bisphosphate to yeast pyruvate kinase.
type: BibliographicResource
authors:
  item: Murcott TH
  item: Gutfreund H
  item: Muirhead H
journal: EMBO J
pages: 3811-4
published year: 1992
volume: 11
references: http://www.ncbi.nlm.nih.gov/pubmed/1396575

Conformation of MgATP bound to nucleotidyl and phosphoryl transfer enzymes 1H-transferred NOE measurements on complexes of methionyl tRNA synthetase and pyruvate kinase.
type: BibliographicResource
authors:
  item: Landy SB
  item: Ray BD
  item: Plateau P
  item: Lipkowitz KB
  item: Rao BD
journal: Eur J Biochem
pages: 59-69
published year: 1992
volume: 205
references: http://www.ncbi.nlm.nih.gov/pubmed/1555604

Cysteinyl peptides labeled by dibromobutanedione in reaction with rabbit muscle pyruvate kinase.
type: BibliographicResource
authors:
  item: Vollmer SH
  item: Colman RF
journal: Protein Sci
pages: 678-87
published year: 1992
volume: 1
references: http://www.ncbi.nlm.nih.gov/pubmed/1304366

Stereochemistry of metal ion coordination to the terminal thiophosphoryl group of adenosine 5'-O-(3-thiotriphosphate) at the active site of pyruvate kinase.
type: BibliographicResource
authors:
  item: Buchbinder JL
  item: Baraniak J
  item: Frey PA
  item: Reed GH
journal: Biochemistry
pages: 14111-6
published year: 1993
volume: 32
references: http://www.ncbi.nlm.nih.gov/pubmed/8260493

Two-dimensional transferred nuclear Overhauser effect spectroscopy study of the confirmation of MgATP bound at the active and ancillary sites of rabbit muscle pyruvate kinase.
type: BibliographicResource
authors:
  item: Jarori GK
  item: Murali N
  item: Rao BD
journal: Biochemistry
pages: 6784-91
published year: 1994
volume: 33
references: http://www.ncbi.nlm.nih.gov/pubmed/8204612

Structure of rabbit muscle pyruvate kinase complexed with Mn2+, K+, and pyruvate.
type: BibliographicResource
authors:
  item: Larsen TM
  item: Laughlin LT
  item: Holden HM
  item: Rayment I
  item: Reed GH
journal: Biochemistry
pages: 6301-9
published year: 1994
volume: 33
references: http://www.ncbi.nlm.nih.gov/pubmed/8193145

Crystal structure of Escherichia coli pyruvate kinase type I: molecular basis of the allosteric transition.
type: BibliographicResource
authors:
  item: Mattevi A
  item: Valentini G
  item: Rizzi M
  item: Speranza ML
  item: Bolognesi M
  item: Coda A
journal: Structure
medline id: 96000862
pages: 729-41
published year: 1995
volume: 3
references: http://www.ncbi.nlm.nih.gov/pubmed/8591049
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P0AD61
comment: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS)

Refined three-dimensional structure of cat-muscle (M1) pyruvate kinase at a resolution of 2.6 A.
type: BibliographicResource
authors:
  item: Allen SC
  item: Muirhead H
journal: Acta Crystallogr D Biol Crystallogr
pages: 499-504
published year: 1996
volume: 52
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P11979
comment: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS)

Three-dimensional structure of cat muscle pyruvate kinase at 3-1 A resolution.
type: BibliographicResource
authors:
  item: Stammers DK
  item: Muirhead H
journal: J Mol Biol
medline id: 77209973
pages: 309-16
published year: 1977
volume: 112
references: http://www.ncbi.nlm.nih.gov/pubmed/875020
references: P11979
comment: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS)

The allosteric regulation of pyruvate kinase.
type: BibliographicResource
authors:
  item: Mattevi A
  item: Bolognesi M
  item: Valentini G
journal: FEBS Lett
pages: 15-9
published year: 1996
volume: 389
references: http://www.ncbi.nlm.nih.gov/pubmed/8682196

Effects of conserved residues on the regulation of rabbit muscle pyruvate kinase.
type: BibliographicResource
authors:
  item: Cheng X
  item: Friesen RH
  item: Lee JC
journal: J Biol Chem
pages: 6313-21
published year: 1996
volume: 271
references: http://www.ncbi.nlm.nih.gov/pubmed/8626426

Ligand-induced conformational changes in wild-type and mutant yeast pyruvate kinase.
type: BibliographicResource
authors:
  item: Collins RA
  item: Kelly SM
  item: Price NC
  item: Fothergill-Gilmore LA
  item: Muirhead H
journal: Protein Eng
pages: 1203-10
published year: 1996
volume: 9
references: http://www.ncbi.nlm.nih.gov/pubmed/9010934

Ligand-induced domain movement in pyruvate kinase: structure of the enzyme from rabbit muscle with Mg2+, K+, and L-phospholactate at 2.7 A resolution.
type: BibliographicResource
authors:
  item: Larsen TM
  item: Benning MM
  item: Wesenberg GE
  item: Rayment I
  item: Reed GH
journal: Arch Biochem Biophys
medline id: 97452476
pages: 199-206
published year: 1997
volume: 345
references: http://www.ncbi.nlm.nih.gov/pubmed/9308890
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P11974
comment: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS)

Allostery in rabbit pyruvate kinase: development of a strategy to elucidate the mechanism.
type: BibliographicResource
authors:
  item: Friesen RH
  item: Castellani RJ
  item: Lee JC
  item: Braun W
journal: Biochemistry
pages: 15266-76
published year: 1998
volume: 37
references: http://www.ncbi.nlm.nih.gov/pubmed/9799487

Structure of the bis(Mg2+)-ATP-oxalate complex of the rabbit muscle pyruvate kinase at 2.1 A resolution: ATP binding over a barrel.
type: BibliographicResource
authors:
  item: Larsen TM
  item: Benning MM
  item: Rayment I
  item: Reed GH
journal: Biochemistry
medline id: 98241346
pages: 6247-55
published year: 1998
volume: 37
references: http://www.ncbi.nlm.nih.gov/pubmed/9572839
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P11974
comment: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS)

Cooperativity in Bacillus stearothermophilus pyruvate kinase.
type: BibliographicResource
authors:
  item: Lovell SC
  item: Mullick AH
  item: Muirhead H
journal: J Mol Biol
pages: 839-51
published year: 1998
volume: 276
references: http://www.ncbi.nlm.nih.gov/pubmed/9500921

The allosteric regulation of pyruvate kinase by fructose-1,6-bisphosphate.
type: BibliographicResource
authors:
  item: Jurica MS
  item: Mesecar A
  item: Heath PJ
  item: Shi W
  item: Nowak T
  item: Stoddard BL
journal: Structure
medline id: 98179936
pages: 195-210
published year: 1998
volume: 6
references: http://www.ncbi.nlm.nih.gov/pubmed/9519410
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P00549
comment: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS)

Structure of pyruvate kinase and similarities with other enzymes: possible implications for protein taxonomy and evolution.
type: BibliographicResource
authors:
  item: Levine M
  item: Muirhead H
  item: Stammers DK
  item: Stuart DI
journal: Nature
pages: 626-30
published year: 1978
volume: 271
references: http://www.ncbi.nlm.nih.gov/pubmed/625331

Role of lysine 240 in the mechanism of yeast pyruvate kinase catalysis.
type: BibliographicResource
authors:
  item: Bollenbach TJ
  item: Mesecar AD
  item: Nowak T
journal: Biochemistry
pages: 9137-45
published year: 1999
volume: 38
references: http://www.ncbi.nlm.nih.gov/pubmed/10413488

The structure of pyruvate kinase from Leishmania mexicana reveals details of the allosteric transition and unusual effector specificity.
type: BibliographicResource
authors:
  item: Rigden DJ
  item: Phillips SE
  item: Michels PA
  item: Fothergill-Gilmore LA
journal: J Mol Biol
medline id: 99380407
pages: 615-35
published year: 1999
volume: 291
references: http://www.ncbi.nlm.nih.gov/pubmed/10448041
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: Q27686
comment: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS)

Anion-induced folding of rabbit muscle pyruvate kinase: existence of multiple intermediate conformations at low pH.
type: BibliographicResource
authors:
  item: Edwin F
  item: Jagannadham MV
journal: Arch Biochem Biophys
pages: 99-110
published year: 2000
volume: 381
references: http://www.ncbi.nlm.nih.gov/pubmed/11019825

Leishmania pyruvate kinase: the crystal structure reveals the structural basis of its unique regulatory properties.
type: BibliographicResource
authors:
  item: Fothergill-Gillmore LA
  item: Rigden DJ
  item: Michels PA
  item: Phillips SE
journal: Biochem Soc Trans
pages: 186-90
published year: 2000
volume: 28
references: http://www.ncbi.nlm.nih.gov/pubmed/10816124

The allosteric regulation of pyruvate kinase.
type: BibliographicResource
authors:
  item: Valentini G
  item: Chiarelli L
  item: Fortin R
  item: Speranza ML
  item: Galizzi A
  item: Mattevi A
journal: J Biol Chem
medline id: 20309762
pages: 18145-52
published year: 2000
volume: 275
references: http://www.ncbi.nlm.nih.gov/pubmed/10751408
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P0AD61
comment: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS)

Dimethylsulfoxide promotes K+-independent activity of pyruvate kinase and the acquisition of the active catalytic conformation.
type: BibliographicResource
authors:
  item: Ramirez-Silva L
  item: Ferreira ST
  item: Nowak T
  item: Tuena de Gomez-Puyou M
  item: Gomez-Puyou A
journal: Eur J Biochem
pages: 3267-74
published year: 2001
volume: 268
references: http://www.ncbi.nlm.nih.gov/pubmed/11389729

Structural and functional linkages between subunit interfaces in mammalian pyruvate kinase.
type: BibliographicResource
authors:
  item: Wooll JO
  item: Friesen RH
  item: White MA
  item: Watowich SJ
  item: Fox RO
  item: Lee JC
  item: Czerwinski EW
journal: J Mol Biol
pages: 525-40
published year: 2001
volume: 312
references: http://www.ncbi.nlm.nih.gov/pubmed/11563914
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

Kinetic and allosteric consequences of mutations in the subunit and domain interfaces and the allosteric site of yeast pyruvate kinase.
type: BibliographicResource
authors:
  item: Fenton AW
  item: Blair JB
journal: Arch Biochem Biophys
pages: 28-39
published year: 2002
volume: 397
references: http://www.ncbi.nlm.nih.gov/pubmed/11747307

Molecular and regulatory properties of leucoplast pyruvate kinase from Brassica napus (rapeseed) suspension cells.
type: BibliographicResource
authors:
  item: Plaxton WC
  item: Smith CR
  item: Knowles VL
journal: Arch Biochem Biophys
pages: 54-62
published year: 2002
volume: 400
references: http://www.ncbi.nlm.nih.gov/pubmed/11913971

Structure and function of human erythrocyte pyruvate kinase. Molecular basis of nonspherocytic hemolytic anemia.
type: BibliographicResource
authors:
  item: Valentini G
  item: Mattevi A
  item: Chiarelli LR
  item: Fortin R
  item: Dolzan M
  item: Galizzi A
  item: Abraham DJ
  item: Wang C
  item: Bianchi P
  item: Zanella A
journal: J Biol Chem
pages: 23807-14
published year: 2002
volume: 277
references: http://www.ncbi.nlm.nih.gov/pubmed/11960989
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Crystal structure of cat muscle pyruvate kinase at a resolution of 2.6 A.
type: BibliographicResource
authors:
  item: Stuart DI
  item: Levine M
  item: Muirhead H
  item: Stammers DK
journal: J Mol Biol
medline id: 80140448
pages: 109-42
published year: 1979
volume: 134
references: http://www.ncbi.nlm.nih.gov/pubmed/537059
references: P11979
comment: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS)

Effects of metabolites on the structural dynamics of rabbit muscle pyruvate kinase.
type: BibliographicResource
authors:
  item: Yu S
  item: Lee LL
  item: Lee JC
journal: Biophys Chem
pages: 1-11
published year: 2003
volume: 103
references: http://www.ncbi.nlm.nih.gov/pubmed/12504250

Monitoring active site alterations upon mutation of yeast pyruvate kinase using 205Tl+ NMR.
type: BibliographicResource
authors:
  item: Susan-Resiga D
  item: Nowak T
journal: J Biol Chem
pages: 40943-52
published year: 2003
volume: 278
references: http://www.ncbi.nlm.nih.gov/pubmed/12882975

Proton donor in yeast pyruvate kinase: chemical and kinetic properties of the active site Thr 298 to Cys mutant.
type: BibliographicResource
authors:
  item: Susan-Resiga D
  item: Nowak T
journal: Biochemistry
pages: 15230-45
published year: 2004
volume: 43
references: http://www.ncbi.nlm.nih.gov/pubmed/15568816

Structural basis for tumor pyruvate kinase M2 allosteric regulation and catalysis.
type: BibliographicResource
authors:
  item: Dombrauckas JD
  item: Santarsiero BD
  item: Mesecar AD
journal: Biochemistry
pages: 9417-29
published year: 2005
volume: 44
references: http://www.ncbi.nlm.nih.gov/pubmed/15996096
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

The structure and function of pyruvate kinase.
type: BibliographicResource
authors:
  item: Muirhead H
  item: Grant JP
  item: Lawton MA
  item: Midwinter CA
  item: Nocton JC
  item: Stuart DI
journal: Biochem Soc Trans
pages: 212-3
published year: 1981
volume: 9
references: http://www.ncbi.nlm.nih.gov/pubmed/7274544

Muscle and liver pyruvate kinases are closely related: amino acid sequence comparisons.
type: BibliographicResource
authors:
  item: Hoar CG
  item: Nicoll GW
  item: Schiltz E
  item: Schmitt W
  item: Bloxham DP
  item: Byford MF
  item: Dunbar B
  item: Fothergill LA
journal: FEBS Lett
pages: 293-6
published year: 1984
volume: 171
references: http://www.ncbi.nlm.nih.gov/pubmed/6723988

Fluorine NMR studies on stereochemical aspects of reactions catalyzed by transcarboxylase, pyruvate kinase, and enzyme I.
type: BibliographicResource
authors:
  item: Hoving H
  item: Crysell B
  item: Leadlay PF
journal: Biochemistry
pages: 6163-9
published year: 1985
volume: 24
references: http://www.ncbi.nlm.nih.gov/pubmed/3910092

7Li, 31P, and 1H NMR studies of interactions between ATP, monovalent cations, and divalent cation sites on rabbit muscle pyruvate kinase.
type: BibliographicResource
authors:
  item: Van Divender JM
  item: Grisham CM
journal: J Biol Chem
pages: 14060-9
published year: 1985
volume: 260
references: http://www.ncbi.nlm.nih.gov/pubmed/2997192

Identification of tyrosine and lysine peptides labeled by 5'-p-fluorosulfonylbenzoyl adenosine in the active site of pyruvate kinase.
type: BibliographicResource
authors:
  item: DeCamp DL
  item: Colman RF
journal: J Biol Chem
pages: 4499-503
published year: 1986
volume: 261
references: http://www.ncbi.nlm.nih.gov/pubmed/3082867

The monovalent cation requirement of rabbit muscle pyruvate kinase is eliminated by substitution of lysine for glutamate 117.
type: BibliographicResource
authors:
  item: Laughlin LT
  item: Reed GH
journal: Arch Biochem Biophys
pages: 262-7
published year: 1997
volume: 348
references: http://www.ncbi.nlm.nih.gov/pubmed/9434737

Conformational changes in yeast pyruvate kinase studied by 205Tl+ NMR.
type: BibliographicResource
authors:
  item: Loria JP
  item: Nowak T
journal: Biochemistry
pages: 6967-74
published year: 1998
volume: 37
references: http://www.ncbi.nlm.nih.gov/pubmed/9578583

1a49A02
type: Pdb
catalytic residue: ARG 72;LYS 269;THR 327;SER 361;GLU 363
cofactor binding residue: ASN 74;SER 76;ASP 112;THR 113(Potassium);GLU 271;ASP 295(Magnesium)
references: 1a49
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1a49

1a49C02
type: Pdb
catalytic residue: ARG 1272;LYS 1469;THR 1527;SER 1561;GLU 1563
cofactor binding residue: ASN 1274;SER 1276;ASP 1312;THR 1313(Potassium);GLU 1471;ASP 1495(Magnesium)
references: 1a49
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1a49

1a49D02
type: Pdb
catalytic residue: ARG 1872;LYS 2069;THR 2127;SER 2161;GLU 2163
cofactor binding residue: ASN 1874;SER 1876;ASP 1912;THR 1913(Potassium);GLU 2071;ASP 2095(Magnesium)
references: 1a49
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1a49

1a49E02
type: Pdb
catalytic residue: ARG 3072;LYS 3269;THR 3327;SER 3361;GLU 3363
cofactor binding residue: ASN 3074;SER 3076;ASP 3112;THR 3113(Potassium);GLU 3271;ASP 3295(Magnesium)
references: 1a49
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1a49

1a49F02
type: Pdb
catalytic residue: ARG 3672;LYS 3869;THR 3927;SER 3961;GLU 3963
cofactor binding residue: ASN 3674;SER 3676;ASP 3712;THR 3713(Potassium);GLU 3871;ASP 3895(Magnesium)
references: 1a49
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1a49

1a49G02
type: Pdb
catalytic residue: ARG 4272;LYS 4469;THR 4527;SER 4561;GLU 4563
cofactor binding residue: ASN 4274;SER 4276;ASP 4312;THR 4313(Potassium);GLU 4471;ASP 4495(Magnesium)
references: 1a49
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1a49

1aqfA02
type: Pdb
catalytic residue: ARG 72;LYS 269;THR 327;SER 361;GLU 363
cofactor binding residue: ASN 74;SER 76;ASP 112;THR 113(Potassium);GLU 271;ASP 295(Magnesium)
references: 1aqf
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1aqf

1aqfB02
type: Pdb
catalytic residue: ARG 72;LYS 269;THR 327;SER 361;GLU 363
cofactor binding residue: ASN 74;SER 76;ASP 112;THR 113(Potassium);GLU 271;ASP 295(Magnesium)
references: 1aqf
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1aqf

1aqfC02
type: Pdb
catalytic residue: ARG 72;LYS 269;THR 327;SER 361;GLU 363
cofactor binding residue: ASN 74;SER 76;ASP 112;THR 113(Potassium);GLU 271;ASP 295(Magnesium)
references: 1aqf
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1aqf

1aqfD02
type: Pdb
catalytic residue: ARG 72;LYS 269;THR 327;SER 361;GLU 363
cofactor binding residue: ASN 74;SER 76;ASP 112;THR 113(Potassium);GLU 271;ASP 295(Magnesium)
references: 1aqf
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1aqf

1aqfE02
type: Pdb
catalytic residue: ARG 72;LYS 269;THR 327;SER 361;GLU 363
cofactor binding residue: ASN 74;SER 76;ASP 112;THR 113(Potassium);GLU 271;ASP 295(Magnesium)
references: 1aqf
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1aqf

1aqfF02
type: Pdb
catalytic residue: ARG 72;LYS 269;THR 327;SER 361;GLU 363
cofactor binding residue: ASN 74;SER 76;ASP 112;THR 113(Potassium);GLU 271;ASP 295(Magnesium)
references: 1aqf
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1aqf

1aqfG02
type: Pdb
catalytic residue: ARG 72;LYS 269;THR 327;SER 361;GLU 363
cofactor binding residue: ASN 74;SER 76;ASP 112;THR 113(Potassium);GLU 271;ASP 295(Magnesium)
references: 1aqf
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1aqf

1aqfH02
type: Pdb
catalytic residue: ARG 72;LYS 269;THR 327;SER 361;GLU 363
cofactor binding residue: ASN 74;SER 76;ASP 112;THR 113(Potassium);GLU 271;ASP 295(Magnesium)
references: 1aqf
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1aqf

1a49B02
type: Pdb
catalytic residue: ARG 672;LYS 869;THR 927;SER 961;GLU 963
cofactor binding residue: ASN 674;SER 676;ASP 712;THR 713(Potassium);GLU 871;ASP 895(Magnesium)
references: 1a49
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1a49

1a49H02
type: Pdb
catalytic residue: ARG 4872;LYS 5069;THR 5127;SER 5161;GLU 5163
cofactor binding residue: ASN 4874;SER 4876;ASP 4912;THR 4913(Potassium);GLU 5071;ASP 5095(Magnesium)
references: 1a49
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1a49

1a5uA02
type: Pdb
catalytic residue: ARG 72;LYS 269;THR 327;SER 361;GLU 363
cofactor binding residue: ASN 74;SER 76;ASP 112;THR 113(Potassium);GLU 271;ASP 295(Magnesium)
references: 1a5u
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1a5u

1a5uC02
type: Pdb
catalytic residue: ARG 1272;LYS 1469;THR 1527;SER 1561;GLU 1563
cofactor binding residue: ASN 1274;SER 1276;ASP 1312;THR 1313(Potassium);GLU 1471;ASP 1495(Magnesium)
references: 1a5u
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1a5u

1a5uD02
type: Pdb
catalytic residue: ARG 1872;LYS 2069;THR 2127;SER 2161;GLU 2163
cofactor binding residue: ASN 1874;SER 1876;ASP 1912;THR 1913(Potassium);GLU 2071;ASP 2095(Magnesium)
references: 1a5u
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1a5u

1a5uE02
type: Pdb
catalytic residue: ARG 3072;LYS 3269;THR 3327;SER 3361;GLU 3363
cofactor binding residue: ASN 3074;SER 3076;ASP 3112;THR 3113(Potassium);GLU 3271;ASP 3295(Magnesium)
references: 1a5u
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1a5u

1a5uF02
type: Pdb
catalytic residue: ARG 3672;LYS 3869;THR 3927;SER 3961;GLU 3963
cofactor binding residue: ASN 3674;SER 3676;ASP 3712;THR 3713(Potassium);GLU 3871;ASP 3895(Magnesium)
references: 1a5u
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1a5u

1a5uG02
type: Pdb
catalytic residue: ARG 4272;LYS 4469;THR 4527;SER 4561;GLU 4563
cofactor binding residue: ASN 4274;SER 4276;ASP 4312;THR 4313(Potassium);GLU 4471;ASP 4495(Magnesium)
references: 1a5u
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1a5u

1f3wA02
type: Pdb
catalytic residue: ARG 72;LYS 269;THR 327;SER 361;GLU 363
cofactor binding residue: ASN 74;SER 76;ASP 112;THR 113(Potassium);GLU 271;ASP 295(Magnesium)
references: 1f3w
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1f3w

1f3wB02
type: Pdb
catalytic residue: ARG 72;LYS 269;THR 327;SER 361;GLU 363
cofactor binding residue: ASN 74;SER 76;ASP 112;THR 113(Potassium);GLU 271;ASP 295(Magnesium)
references: 1f3w
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1f3w

1f3wC02
type: Pdb
catalytic residue: ARG 72;LYS 269;THR 327;SER 361;GLU 363
cofactor binding residue: ASN 74;SER 76;ASP 112;THR 113(Potassium);GLU 271;ASP 295(Magnesium)
references: 1f3w
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1f3w

1f3wD02
type: Pdb
catalytic residue: ARG 72;LYS 269;THR 327;SER 361;GLU 363
cofactor binding residue: ASN 74;SER 76;ASP 112;THR 113(Potassium);GLU 271;ASP 295(Magnesium)
references: 1f3w
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1f3w

1f3wE02
type: Pdb
catalytic residue: ARG 72;LYS 269;THR 327;SER 361;GLU 363
cofactor binding residue: ASN 74;SER 76;ASP 112;THR 113(Potassium);GLU 271;ASP 295(Magnesium)
references: 1f3w
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1f3w

1f3wF02
type: Pdb
catalytic residue: ARG 72;LYS 269;THR 327;SER 361;GLU 363
cofactor binding residue: ASN 74;SER 76;ASP 112;THR 113(Potassium);GLU 271;ASP 295(Magnesium)
references: 1f3w
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1f3w

1f3wG02
type: Pdb
catalytic residue: ARG 72;LYS 269;THR 327;SER 361;GLU 363
cofactor binding residue: ASN 74;SER 76;ASP 112;THR 113(Potassium);GLU 271;ASP 295(Magnesium)
references: 1f3w
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1f3w

1f3wH02
type: Pdb
catalytic residue: ARG 72;LYS 269;THR 327;SER 361;GLU 363
cofactor binding residue: ASN 74;SER 76;ASP 112;THR 113(Potassium);GLU 271;ASP 295(Magnesium)
references: 1f3w
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1f3w

1f3xA02
type: Pdb
catalytic residue: ARG 72;LYS 269;THR 327;SER 361;GLU 363
cofactor binding residue: ASN 74;SER 76;ASP 112;THR 113(Potassium);GLU 271;ASP 295(Manganese)
references: 1f3x
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1f3x

1f3xB02
type: Pdb
catalytic residue: ARG 72;LYS 269;THR 327;SER 361;GLU 363
cofactor binding residue: ASN 74;SER 76;ASP 112;THR 113(Potassium);GLU 271;ASP 295(Manganese)
references: 1f3x
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1f3x

1f3xC02
type: Pdb
catalytic residue: ARG 72;LYS 269;THR 327;SER 361;GLU 363
cofactor binding residue: ASN 74;SER 76;ASP 112;THR 113(Potassium);GLU 271;ASP 295(Manganese)
references: 1f3x
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1f3x

1f3xD02
type: Pdb
catalytic residue: ARG 72;LYS 269;THR 327;SER 361;GLU 363
cofactor binding residue: ASN 74;SER 76;ASP 112;THR 113(Potassium);GLU 271;ASP 295(Manganese)
references: 1f3x
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1f3x

1f3xE02
type: Pdb
catalytic residue: ARG 72;LYS 269;THR 327;SER 361;GLU 363
cofactor binding residue: ASN 74;SER 76;ASP 112;THR 113(Potassium);GLU 271;ASP 295(Manganese)
references: 1f3x
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1f3x

1f3xF02
type: Pdb
catalytic residue: ARG 72;LYS 269;THR 327;SER 361;GLU 363
cofactor binding residue: ASN 74;SER 76;ASP 112;THR 113(Potassium);GLU 271;ASP 295(Manganese)
references: 1f3x
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1f3x

1f3xG02
type: Pdb
catalytic residue: ARG 72;LYS 269;THR 327;SER 361;GLU 363
cofactor binding residue: ASN 74;SER 76;ASP 112;THR 113(Potassium);GLU 271;ASP 295(Manganese)
references: 1f3x
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1f3x

1f3xH02
type: Pdb
catalytic residue: ARG 72;LYS 269;THR 327;SER 361;GLU 363
cofactor binding residue: ASN 74;SER 76;ASP 112;THR 113(Potassium);GLU 271;ASP 295(Manganese)
references: 1f3x
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1f3x

1pknA02
type: Pdb
catalytic residue: ARG 72;LYS 269;THR 327;SER 361;GLU 363
cofactor binding residue: ASN 74;SER 76;ASP 112;THR 113(Potassium);GLU 271;ASP 295(Manganese)
references: 1pkn
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1pkn

1t5aA02
type: Pdb
catalytic residue: ARG 73;LYS 270;THR 328;SER 362;GLU 364
cofactor binding residue: ASN 75;SER 77;ASP 113;THR 114(Potassium);GLU 272;ASP 296(Magnesium)
references: 1t5a
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1t5a

1t5aB02
type: Pdb
catalytic residue: ARG 73;LYS 270;THR 328;SER 362;GLU 364
cofactor binding residue: ASN 75;SER 77;ASP 113;THR 114(Potassium);GLU 272;ASP 296(Magnesium)
references: 1t5a
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1t5a

1t5aC02
type: Pdb
catalytic residue: ARG 73;LYS 270;THR 328;SER 362;GLU 364
cofactor binding residue: ASN 75;SER 77;ASP 113;THR 114(Potassium);GLU 272;ASP 296(Magnesium)
references: 1t5a
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1t5a

1t5aD02
type: Pdb
catalytic residue: ARG 73;LYS 270;THR 328;SER 362;GLU 364
cofactor binding residue: ASN 75;SER 77;ASP 113;THR 114(Potassium);GLU 272;ASP 296(Magnesium)
references: 1t5a
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1t5a

1a3wA02
type: Pdb
catalytic residue: ARG 49;LYS 240;THR 298;SER 332;GLU 334
cofactor binding residue: ASN 51;SER 53;ASP 84;THR 85(Potassium);GLU 242;ASP 266(Magnesium)
references: 1a3w
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1a3w

1a3wB02
type: Pdb
catalytic residue: ARG 49;LYS 240;THR 298;SER 332;GLU 334
cofactor binding residue: ASN 51;SER 53;ASP 84;THR 85(Potassium);GLU 242;ASP 266(Magnesium)
references: 1a3w
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1a3w

1a3xA02
type: Pdb
catalytic residue: ARG 49;LYS 240;THR 298;SER 332;GLU 334
cofactor binding residue: ASN 51;SER 53;ASP 84;THR 85(Potassium);GLU 242;ASP 266(Magnesium)
references: 1a3x
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1a3x

1a3xB02
type: Pdb
catalytic residue: ARG 49;LYS 240;THR 298;SER 332;GLU 334
cofactor binding residue: ASN 51;SER 53;ASP 84;THR 85(Potassium);GLU 242;ASP 266(Magnesium)
references: 1a3x
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1a3x

1a5uB02
type: Pdb
catalytic residue: ARG 672;LYS 869;THR 927;SER 961;GLU 963
cofactor binding residue: ASN 674;SER 676;ASP 712;THR 713(Potassium);GLU 871;ASP 895(Magnesium)
references: 1a5u
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1a5u

1a5uH02
type: Pdb
catalytic residue: ARG 4872;LYS 5069;THR 5127;SER 5161;GLU 5163
cofactor binding residue: ASN 4874;SER 4876;ASP 4912;THR 4913(Potassium);GLU 5071;ASP 5095(Magnesium)
references: 1a5u
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1a5u

1liuA02
type: Pdb
catalytic residue: ARG 116;LYS 313;THR 371;SER 405;GLU 407
cofactor binding residue: ASN 118;SER 120;ASP 156;THR 157(Potassium);GLU 315;ASP 339(Magnesium)
references: 1liu
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1liu

1liuB02
type: Pdb
catalytic residue: ARG 116;LYS 313;THR 371;SER 405;GLU 407
cofactor binding residue: ASN 118;SER 120;ASP 156;THR 157(Potassium);GLU 315;ASP 339(Magnesium)
references: 1liu
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1liu

1liuC02
type: Pdb
catalytic residue: ARG 116;LYS 313;THR 371;SER 405;GLU 407
cofactor binding residue: ASN 118;SER 120;ASP 156;THR 157(Potassium);GLU 315;ASP 339(Magnesium)
references: 1liu
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1liu

1liuD02
type: Pdb
catalytic residue: ARG 116;LYS 313;THR 371;SER 405;GLU 407
cofactor binding residue: ASN 118;SER 120;ASP 156;THR 157(Potassium);GLU 315;ASP 339(Magnesium)
references: 1liu
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1liu

1liwA02
type: Pdb
catalytic residue: ARG 116;LYS 313;THR 371;SER 405;GLU 407
cofactor binding residue: ASN 118;SER 120;ASP 156;THR 157(Potassium);GLU 315;ASP 339(Magnesium)
references: 1liw
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1liw

1liwB02
type: Pdb
catalytic residue: ARG 116;LYS 313;THR 371;SER 405;GLU 407
cofactor binding residue: ASN 118;SER 120;ASP 156;THR 157(Potassium);GLU 315;ASP 339(Magnesium)
references: 1liw
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1liw

1liwC02
type: Pdb
catalytic residue: ARG 116;LYS 313;THR 371;SER 405;GLU 407
cofactor binding residue: ASN 118;SER 120;ASP 156;THR 157(Potassium);GLU 315;ASP 339(Magnesium)
references: 1liw
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1liw

1liwD02
type: Pdb
catalytic residue: ARG 116;LYS 313;THR 371;SER 405;GLU 407
cofactor binding residue: ASN 118;SER 120;ASP 156;THR 157(Potassium);GLU 315;ASP 339(Magnesium)
references: 1liw
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1liw

1lixA02
type: Pdb
catalytic residue: ARG 116;LYS 313;THR 371;SER 405;GLU 407
cofactor binding residue: ASN 118;SER 120;ASP 156;THR 157(Potassium);GLU 315;ASP 339(Magnesium)
references: 1lix
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1lix

1lixB02
type: Pdb
catalytic residue: ARG 116;LYS 313;THR 371;SER 405;GLU 407
cofactor binding residue: ASN 118;SER 120;ASP 156;THR 157(Potassium);GLU 315;ASP 339(Magnesium)
references: 1lix
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1lix

1lixC02
type: Pdb
catalytic residue: ARG 116;LYS 313;THR 371;SER 405;GLU 407
cofactor binding residue: ASN 118;SER 120;ASP 156;THR 157(Potassium);GLU 315;ASP 339(Magnesium)
references: 1lix
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1lix

1lixD02
type: Pdb
catalytic residue: ARG 116;LYS 313;THR 371;SER 405;GLU 407
cofactor binding residue: ASN 118;SER 120;ASP 156;THR 157(Potassium);GLU 315;ASP 339(Magnesium)
references: 1lix
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1lix

1liyA02
type: Pdb
catalytic residue: ARG 116;LYS 313;THR 371;SER 405;GLU 407
cofactor binding residue: ASN 118;SER 120;ASP 156;THR 157(Potassium);GLU 315;ASP 339(Magnesium)
references: 1liy
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1liy

1liyB02
type: Pdb
catalytic residue: ARG 116;LYS 313;THR 371;SER 405;GLU 407
cofactor binding residue: ASN 118;SER 120;ASP 156;THR 157(Potassium);GLU 315;ASP 339(Magnesium)
references: 1liy
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1liy

1liyC02
type: Pdb
catalytic residue: ARG 116;LYS 313;THR 371;SER 405;GLU 407
cofactor binding residue: ASN 118;SER 120;ASP 156;THR 157(Potassium);GLU 315;ASP 339(Magnesium)
references: 1liy
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1liy

1liyD02
type: Pdb
catalytic residue: ARG 116;LYS 313;THR 371;SER 405;GLU 407
cofactor binding residue: ASN 118;SER 120;ASP 156;THR 157(Potassium);GLU 315;ASP 339(Magnesium)
references: 1liy
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1liy

1a3wA03
type: Pdb
catalytic residue: ARG 91
references: 1a3w
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1a3w

1a3wB03
type: Pdb
catalytic residue: ARG 91
references: 1a3w
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1a3w

1a3xA03
type: Pdb
catalytic residue: ARG 91
references: 1a3x
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1a3x

1a3xB03
type: Pdb
catalytic residue: ARG 91
references: 1a3x
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1a3x

1a49A03
type: Pdb
catalytic residue: ARG 119
references: 1a49
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1a49

1a49B03
type: Pdb
catalytic residue: ARG 719
references: 1a49
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1a49

1a49C03
type: Pdb
catalytic residue: ARG 1319
references: 1a49
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1a49

1a49D03
type: Pdb
catalytic residue: ARG 1919
references: 1a49
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1a49

1a49E03
type: Pdb
catalytic residue: ARG 3119
references: 1a49
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1a49

1a49F03
type: Pdb
catalytic residue: ARG 3719
references: 1a49
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1a49

1a49G03
type: Pdb
catalytic residue: ARG 4319
references: 1a49
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1a49

1a49H03
type: Pdb
catalytic residue: ARG 4919
references: 1a49
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1a49

1a5uA03
type: Pdb
catalytic residue: ARG 119
references: 1a5u
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1a5u

1a5uB03
type: Pdb
catalytic residue: ARG 719
references: 1a5u
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1a5u

1a5uC03
type: Pdb
catalytic residue: ARG 1319
references: 1a5u
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1a5u

1a5uD03
type: Pdb
catalytic residue: ARG 1919
references: 1a5u
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1a5u

1a5uE03
type: Pdb
catalytic residue: ARG 3119
references: 1a5u
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1a5u

1a5uF03
type: Pdb
catalytic residue: ARG 3719
references: 1a5u
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1a5u

1a5uG03
type: Pdb
catalytic residue: ARG 4319
references: 1a5u
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1a5u

1a5uH03
type: Pdb
catalytic residue: ARG 4919
references: 1a5u
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1a5u

1aqfA03
type: Pdb
catalytic residue: ARG 119
references: 1aqf
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1aqf

1aqfB03
type: Pdb
catalytic residue: ARG 119
references: 1aqf
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1aqf

1aqfC03
type: Pdb
catalytic residue: ARG 119
references: 1aqf
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1aqf

1aqfD03
type: Pdb
catalytic residue: ARG 119
references: 1aqf
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1aqf

1aqfF03
type: Pdb
catalytic residue: ARG 119
references: 1aqf
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1aqf

1aqfG03
type: Pdb
catalytic residue: ARG 119
references: 1aqf
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1aqf

1aqfH03
type: Pdb
catalytic residue: ARG 119
references: 1aqf
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1aqf

1e0tA02
type: Pdb
catalytic residue: ARG 32;LYS 220;THR 278;SER 312;GLU 314
cofactor binding residue: ASN 34;SER 36;ASP 66;THR 67(Potassium);GLU 222;ASP 246(Magnesium)
references: 1e0t
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e0t
comment: mutant Q279M, R292D

1e0tA03
type: Pdb
catalytic residue: ARG 73
references: 1e0t
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e0t

1e0tB02
type: Pdb
catalytic residue: ARG 32;LYS 220;THR 278;SER 312;GLU 314
cofactor binding residue: ASN 34;SER 36;ASP 66;THR 67(Potassium);GLU 222;ASP 246(Magnesium)
references: 1e0t
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e0t
comment: mutant Q279M, R292D

1e0tB03
type: Pdb
catalytic residue: ARG 73
references: 1e0t
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e0t

1e0tC02
type: Pdb
catalytic residue: ARG 32;LYS 220;THR 278;SER 312;GLU 314
cofactor binding residue: ASN 34;SER 36;ASP 66;THR 67(Potassium);GLU 222;ASP 246(Magnesium)
references: 1e0t
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e0t
comment: mutant Q279M, R292D

1e0tC03
type: Pdb
catalytic residue: ARG 73
references: 1e0t
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e0t

1e0tD02
type: Pdb
catalytic residue: ARG 32;LYS 220;THR 278;SER 312;GLU 314
cofactor binding residue: ASN 34;SER 36;ASP 66;THR 67(Potassium);GLU 222;ASP 246(Magnesium)
references: 1e0t
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e0t
comment: mutant Q279M, R292D

1e0tD03
type: Pdb
catalytic residue: ARG 73
references: 1e0t
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e0t

1e0uA02
type: Pdb
catalytic residue: ARG 32;LYS 220;THR 278;SER 312;GLU 314
cofactor binding residue: ASN 34;SER 36;ASP 66;THR 67(Potassium);GLU 222;ASP 246(Magnesium)
references: 1e0u
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e0u
comment: mutant R271L, Q279M

1e0uA03
type: Pdb
catalytic residue: ARG 73
references: 1e0u
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e0u

1e0uB02
type: Pdb
catalytic residue: ARG 32;LYS 220;THR 278;SER 312;GLU 314
cofactor binding residue: ASN 34;SER 36;ASP 66;THR 67(Potassium);GLU 222;ASP 246(Magnesium)
references: 1e0u
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e0u
comment: mutant R271L, Q279M

1e0uB03
type: Pdb
catalytic residue: ARG 73
references: 1e0u
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e0u

1e0uC02
type: Pdb
catalytic residue: ARG 32;LYS 220;THR 278;SER 312;GLU 314
cofactor binding residue: ASN 34;SER 36;ASP 66;THR 67(Potassium);GLU 222;ASP 246(Magnesium)
references: 1e0u
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e0u
comment: mutant R271L, Q279M

1e0uC03
type: Pdb
catalytic residue: ARG 73
references: 1e0u
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e0u

1e0uD02
type: Pdb
catalytic residue: ARG 32;LYS 220;THR 278;SER 312;GLU 314
cofactor binding residue: ASN 34;SER 36;ASP 66;THR 67(Potassium);GLU 222;ASP 246(Magnesium)
references: 1e0u
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e0u
comment: mutant R271L, Q279M

1e0uD03
type: Pdb
catalytic residue: ARG 73
references: 1e0u
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1e0u

1f3wA03
type: Pdb
catalytic residue: ARG 119
references: 1f3w
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1f3w

1f3wB03
type: Pdb
catalytic residue: ARG 119
references: 1f3w
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1f3w

1f3wC03
type: Pdb
catalytic residue: ARG 119
references: 1f3w
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1f3w

1f3wD03
type: Pdb
catalytic residue: ARG 119
references: 1f3w
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1f3w

1f3wE03
type: Pdb
catalytic residue: ARG 119
references: 1f3w
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1f3w

1f3wF03
type: Pdb
catalytic residue: ARG 119
references: 1f3w
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1f3w

1f3wG03
type: Pdb
catalytic residue: ARG 119
references: 1f3w
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1f3w

1f3wH03
type: Pdb
catalytic residue: ARG 119
references: 1f3w
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1f3w

1f3xA01
type: Pdb
references: 1f3x
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1f3x
comment: mutant S402P

1f3xA03
type: Pdb
catalytic residue: ARG 119
references: 1f3x
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1f3x

1f3xB01
type: Pdb
references: 1f3x
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1f3x
comment: mutant S402P

1f3xB03
type: Pdb
catalytic residue: ARG 119
references: 1f3x
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1f3x

1f3xC01
type: Pdb
references: 1f3x
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1f3x
comment: mutant S402P

1f3xC03
type: Pdb
catalytic residue: ARG 119
references: 1f3x
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1f3x

1f3xD01
type: Pdb
references: 1f3x
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1f3x
comment: mutant S402P

1f3xD03
type: Pdb
catalytic residue: ARG 119
references: 1f3x
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1f3x

1f3xE01
type: Pdb
references: 1f3x
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1f3x
comment: mutant S402P

1f3xE03
type: Pdb
catalytic residue: ARG 119
references: 1f3x
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1f3x

1f3xF01
type: Pdb
references: 1f3x
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1f3x
comment: mutant S402P

1f3xF03
type: Pdb
catalytic residue: ARG 119
references: 1f3x
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1f3x

1f3xG01
type: Pdb
references: 1f3x
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1f3x
comment: mutant S402P

1f3xG03
type: Pdb
catalytic residue: ARG 119
references: 1f3x
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1f3x

1f3xH01
type: Pdb
references: 1f3x
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1f3x
comment: mutant S402P

1f3xH03
type: Pdb
catalytic residue: ARG 119
references: 1f3x
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1f3x

1liuA03
type: Pdb
catalytic residue: ARG 163
references: 1liu
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1liu

1liuB03
type: Pdb
catalytic residue: ARG 163
references: 1liu
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1liu

1liuC03
type: Pdb
catalytic residue: ARG 163
references: 1liu
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1liu

1liuD03
type: Pdb
catalytic residue: ARG 163
references: 1liu
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1liu

1liwA03
type: Pdb
catalytic residue: ARG 163
references: 1liw
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1liw

1liwB03
type: Pdb
catalytic residue: ARG 163
references: 1liw
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1liw

1liwC03
type: Pdb
catalytic residue: ARG 163
references: 1liw
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1liw

1liwD03
type: Pdb
catalytic residue: ARG 163
references: 1liw
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1liw

1lixA03
type: Pdb
catalytic residue: ARG 163
references: 1lix
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1lix

1lixB03
type: Pdb
catalytic residue: ARG 163
references: 1lix
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1lix

1lixC03
type: Pdb
catalytic residue: ARG 163
references: 1lix
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1lix

1lixD03
type: Pdb
catalytic residue: ARG 163
references: 1lix
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1lix

1liyA03
type: Pdb
catalytic residue: ARG 163
references: 1liy
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1liy

1liyB03
type: Pdb
catalytic residue: ARG 163
references: 1liy
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1liy

1liyC03
type: Pdb
catalytic residue: ARG 163
references: 1liy
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1liy

1liyD03
type: Pdb
catalytic residue: ARG 163
references: 1liy
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1liy

1pklA02
type: Pdb
catalytic residue: ARG 49;LYS 238;THR 296;SER 330;GLU 332
cofactor binding residue: ASN 51;SER 53;ASP 83;THR 84(Potassium);GLU 240;ASP 264(Magnesium)
references: 1pkl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1pkl

1pklA03
type: Pdb
catalytic residue: ARG 90
references: 1pkl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1pkl

1pklB02
type: Pdb
catalytic residue: ARG 49;LYS 238;THR 296;SER 330;GLU 332
cofactor binding residue: ASN 51;SER 53;ASP 83;THR 84(Potassium);GLU 240;ASP 264(Magnesium)
references: 1pkl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1pkl

1pklB03
type: Pdb
catalytic residue: ARG 90
references: 1pkl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1pkl

1pklC02
type: Pdb
catalytic residue: ARG 49;LYS 238;THR 296;SER 330;GLU 332
cofactor binding residue: ASN 51;SER 53;ASP 83;THR 84(Potassium);GLU 240;ASP 264(Magnesium)
references: 1pkl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1pkl

1pklC03
type: Pdb
catalytic residue: ARG 90
references: 1pkl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1pkl

1pklD02
type: Pdb
catalytic residue: ARG 49;LYS 238;THR 296;SER 330;GLU 332
cofactor binding residue: ASN 51;SER 53;ASP 83;THR 84(Potassium);GLU 240;ASP 264(Magnesium)
references: 1pkl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1pkl

1pklD03
type: Pdb
catalytic residue: ARG 90
references: 1pkl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1pkl

1pklE02
type: Pdb
catalytic residue: ARG 49;LYS 238;THR 296;SER 330;GLU 332
cofactor binding residue: ASN 51;SER 53;ASP 83;THR 84(Potassium);GLU 240;ASP 264(Magnesium)
references: 1pkl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1pkl

1pklE03
type: Pdb
catalytic residue: ARG 90
references: 1pkl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1pkl

1pklF02
type: Pdb
catalytic residue: ARG 49;LYS 238;THR 296;SER 330;GLU 332
cofactor binding residue: ASN 51;SER 53;ASP 83;THR 84(Potassium);GLU 240;ASP 264(Magnesium)
references: 1pkl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1pkl

1pklF03
type: Pdb
catalytic residue: ARG 90
references: 1pkl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1pkl

1pklG02
type: Pdb
catalytic residue: ARG 49;LYS 238;THR 296;SER 330;GLU 332
cofactor binding residue: ASN 51;SER 53;ASP 83;THR 84(Potassium);GLU 240;ASP 264(Magnesium)
references: 1pkl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1pkl

1pklG03
type: Pdb
catalytic residue: ARG 90
references: 1pkl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1pkl

1pklH02
type: Pdb
catalytic residue: ARG 49;LYS 238;THR 296;SER 330;GLU 332
cofactor binding residue: ASN 51;SER 53;ASP 83;THR 84(Potassium);GLU 240;ASP 264(Magnesium)
references: 1pkl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1pkl

1pklH03
type: Pdb
catalytic residue: ARG 90
references: 1pkl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1pkl

1pkmA02
type: Pdb
catalytic residue: ARG 72;LYS 269;THR 327;SER 361;GLU 363
cofactor binding residue: ASN 74;SER 76;ASP 112;THR 113(Potassium);GLU 271;ASP 295(Magnesium)
references: 1pkm
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1pkm

1pkmA03
type: Pdb
catalytic residue: ARG 119
references: 1pkm
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1pkm

1pknA03
type: Pdb
catalytic residue: ARG 119
references: 1pkn
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1pkn

1pkyA02
type: Pdb
catalytic residue: ARG 32;LYS 220;THR 278;SER 312;GLU 314
cofactor binding residue: ASN 34;SER 36;ASP 66;THR 67(Potassium);GLU 222;ASP 246(Magnesium)
references: 1pky
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1pky

1pkyA03
type: Pdb
catalytic residue: ARG 73
references: 1pky
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1pky

1pkyB02
type: Pdb
catalytic residue: ARG 32;LYS 220;THR 278;SER 312;GLU 314
cofactor binding residue: ASN 34;SER 36;ASP 66;THR 67(Potassium);GLU 222;ASP 246(Magnesium)
references: 1pky
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1pky

1pkyB03
type: Pdb
catalytic residue: ARG 73
references: 1pky
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1pky

1pkyC02
type: Pdb
catalytic residue: ARG 32;LYS 220;THR 278;SER 312;GLU 314
cofactor binding residue: ASN 34;SER 36;ASP 66;THR 67(Potassium);GLU 222;ASP 246(Magnesium)
references: 1pky
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1pky

1pkyC03
type: Pdb
catalytic residue: ARG 73
references: 1pky
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1pky

1pkyD02
type: Pdb
catalytic residue: ARG 32;LYS 220;THR 278;SER 312;GLU 314
cofactor binding residue: ASN 34;SER 36;ASP 66;THR 67(Potassium);GLU 222;ASP 246(Magnesium)
references: 1pky
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1pky

1pkyD03
type: Pdb
catalytic residue: ARG 73
references: 1pky
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1pky

1t5aA03
type: Pdb
catalytic residue: ARG 120
references: 1t5a
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1t5a

1t5aB03
type: Pdb
catalytic residue: ARG 120
references: 1t5a
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1t5a

1t5aC03
type: Pdb
catalytic residue: ARG 120
references: 1t5a
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1t5a

1t5aD03
type: Pdb
catalytic residue: ARG 120
references: 1t5a
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1t5a

1zjhA02
type: Pdb
catalytic residue: ARG 72;LYS 269;THR 327;SER 361;GLU 363
cofactor binding residue: ASN 74;SER 76;ASP 112;THR 113(Potassium);GLU 271;ASP 295(Magnesium)
references: 1zjh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1zjh

1zjhA03
type: Pdb
catalytic residue: ARG 119
references: 1zjh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1zjh

Potassium
type: KeggCofactor
compound type: univalent metal (Na+, K+)
references: KEGG:C00238
references: CHEBI:29103
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Magnesium
type: KeggCofactor
compound type: divalent metal (Ca2+, Mg2+)
references: KEGG:C00305
references: CHEBI:18420
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Pyruvate
type: KeggProduct
compound type: carbohydrate
compound type: carboxyl group
references: KEGG:C00022
references: CHEBI:32816
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

ATP
type: KeggProduct
compound type: amine group
compound type: nucleotide
references: KEGG:C00002
references: CHEBI:15422
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Phosphoenolpyruvate
type: KeggSubstrate
compound type: carboxyl group
compound type: phosphate group/phosphate ion
references: KEGG:C00074
references: CHEBI:44897
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

ADP
type: KeggSubstrate
compound type: amine group
compound type: nucleotide
references: KEGG:C00008
references: CHEBI:16761
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

phosphoenolpyruvate kinase
type: KeggEnzyme

phosphoenol transphosphorylase
type: KeggEnzyme