M00017
type: Enzyme
active site residues resources: Functional diversity of the phosphoglucomutase superfamily: structural implications.
active site residues resources: Crystal structure of PMM/PGM: an enzyme in the biosynthetic pathway of P. aeruginosa virulence factors.
active site residues resources: Roles of active site residues in Pseudomonas aeruginosa phosphomannomutase/phosphoglucomutase.
cath: Alpha-D-Glucose-1,6-Bisphosphate; Chain A, domain 3
cath: TATA-Binding Protein
ec: https://purl.uniprot.org/enzyme/5.4.2.2
kegg cofactor: Magnesium
kegg enzyme: phosphoglucomutase
kegg intermediate: D-Glucose 1,6-bisphosphate
kegg pathway: Glycolysis / Gluconeogenesis
kegg pathway: Pentose phosphate pathway
kegg pathway: Galactose metabolism
kegg pathway: Starch and sucrose metabolism
kegg pathway: Streptomycin biosynthesis
kegg product: alpha-D-Glucose 6-phosphate
kegg product: alpha-D-Ribose 5-phosphate
kegg product: alpha-D-Hexose 6-phosphate
kegg substrate: alpha-D-Glucose 1-phosphate
kegg substrate: alpha-D-Ribose 1-phosphate
kegg substrate: alpha-D-Hexose 1-phosphate
pdb: 1c47A01
pdb: 1c47B01
pdb: 1c4gA01
pdb: 1c4gB01
pdb: 1jdyA01
pdb: 1jdyB01
pdb: 1lxtA01
pdb: 1lxtB01
pdb: 1vklA01
pdb: 1vklB01
pdb: 2pmgA01
pdb: 2pmgB01
pdb: 3pmgA01
pdb: 3pmgB01
pdb: 1kfiA01
pdb: 1kfiB01
pdb: 1kfqA01
pdb: 1kfqB01
pdb: 1c47A02
pdb: 1c47B02
pdb: 1c4gA02
pdb: 1c4gB02
pdb: 1jdyA02
pdb: 1jdyB02
pdb: 1lxtA02
pdb: 1lxtB02
pdb: 1vklA02
pdb: 1vklB02
pdb: 2pmgA02
pdb: 2pmgB02
pdb: 3pmgA02
pdb: 3pmgB02
pdb: 1kfiA02
pdb: 1kfiB02
pdb: 1kfqA02
pdb: 1kfqB02
pdb: 1c47A03
pdb: 1c47B03
pdb: 1c4gA03
pdb: 1c4gB03
pdb: 1jdyA03
pdb: 1jdyB03
pdb: 1lxtA03
pdb: 1lxtB03
pdb: 1vklA03
pdb: 1vklB03
pdb: 2pmgA03
pdb: 2pmgB03
pdb: 3pmgA03
pdb: 3pmgB03
pdb: 1kfiA03
pdb: 1kfiB03
pdb: 1kfqA03
pdb: 1kfqB03
pdb: 1c47A04
pdb: 1c47B04
pdb: 1c4gA04
pdb: 1c4gB04
pdb: 1jdyA04

Analogue
compound: alpha-D-Glucose 1-phosphate
ligand het code: SO4
pdb: 1jdyA04

Analogue
compound: alpha-D-Glucose 1-phosphate
ligand het code: SO4
pdb: 1jdyB04

Analogue
compound: alpha-D-Glucose 1-phosphate
ligand het code: SO4
pdb: 1kfiA04

Analogue
compound: alpha-D-Glucose 1-phosphate
ligand het code: SO4
pdb: 1kfiB04

Analogue
compound: Magnesium
ligand het code: _CD
pdb: 1c47A02

Analogue
compound: Magnesium
ligand het code: _CD
pdb: 1c47B02

Analogue
compound: Magnesium
ligand het code: _CO
pdb: 1c4gA02

Analogue
compound: Magnesium
ligand het code: _CD
pdb: 1jdyA02

Analogue
compound: Magnesium
ligand het code: _CD
pdb: 1jdyB02

Analogue
compound: Magnesium
ligand het code: _CD
pdb: 1lxtA02

Analogue
compound: Magnesium
ligand het code: _CD
pdb: 1lxtB02

Analogue
compound: Magnesium
ligand het code: _NI
pdb: 1vklA02

Analogue
compound: Magnesium
ligand het code: _NI
pdb: 1vklB02

Analogue
compound: Magnesium
ligand het code: _ZN
pdb: 1kfiA02

Analogue
compound: Magnesium
ligand het code: _ZN
pdb: 1kfiB02

Analogue
compound: Magnesium
ligand het code: _CA
pdb: 1kfqA02

Analogue
compound: Magnesium
ligand het code: _CA
pdb: 1kfqB02

IntermediateBound
compound: D-Glucose 1,6-bisphosphate
ligand het code: G16
pdb: 1c47A03

TransitionStateAnalogue
ligand het code: VG1
pdb: 1c4gA03

ReferenceForCatalyticMechanism
reference index: 9
reference section: Scheme II, p.504

ReferenceForCatalyticMechanism
reference index: 10
reference section: p.511-512

ReferenceForCatalyticMechanism
reference index: 11
reference section: p.6328-6329

ReferenceForCatalyticMechanism
reference index: 12
reference section: p.52-55

ReferenceForCatalyticMechanism
reference index: 14
reference section: p.404-405

ReferenceForCatalyticMechanism
reference index: 16
reference section: p.148

ReferenceForCatalyticMechanism
reference index: 17
reference section: Fig.5, p.275-277

ReferenceForCatalyticMechanism
reference index: 18
reference section: Chart 1, p.9948-9950

ReferenceForCatalyticMechanism
reference index: 19
reference section: Fig.1, p.60-61

TATA-Binding Protein
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.30.310.50

Alpha-D-Glucose-1,6-Bisphosphate; Chain A, domain 3
type: Cath
catalytic domain: index.html
references: http://www.cathdb.info/version/latest/superfamily/3.40.120.10

Glycolysis / Gluconeogenesis
type: KeggPathway
references: KEGG:MAP00010

Pentose phosphate pathway
type: KeggPathway
references: KEGG:MAP00030

Galactose metabolism
type: KeggPathway
references: KEGG:MAP00052

Starch and sucrose metabolism
type: KeggPathway
references: KEGG:MAP00500

Streptomycin biosynthesis
type: KeggPathway
references: KEGG:MAP00521

A tryptic peptide containing a unique serine phosphate residue in rabbit phosphoglucomutase.
type: BibliographicResource
authors:
  item: Milstein CP
  item: Milstein C
journal: Biochem J
medline id: 68368401
pages: 93-9
published year: 1968
volume: 109
references: http://www.ncbi.nlm.nih.gov/pubmed/5669853
references: P00949
comment: ACTIVE SITE

19F NMR investigations of the catalytic mechanism of phosphoglucomutase using fluorinated substrates and inhibitors.
type: BibliographicResource
authors:
  item: Percival MD
  item: Withers SG
journal: Biochemistry
pages: 505-12
published year: 1992
volume: 31
references: http://www.ncbi.nlm.nih.gov/pubmed/1531026

The crystal structure of muscle phosphoglucomutase refined at 2.7-angstrom resolution.
type: BibliographicResource
authors:
  item: Dai JB
  item: Liu Y
  item: Ray WJ Jr
  item: Konno M
journal: J Biol Chem
medline id: 92210613
pages: 6322-37
published year: 1992
volume: 267
references: http://www.ncbi.nlm.nih.gov/pubmed/1532581
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P00949
comment: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS)

Structural changes at the metal ion binding site during the phosphoglucomutase reaction.
type: BibliographicResource
authors:
  item: Ray WJ Jr
  item: Post CB
  item: Liu Y
  item: Rhyu GI
journal: Biochemistry
pages: 48-57
published year: 1993
volume: 32
references: http://www.ncbi.nlm.nih.gov/pubmed/8418859

Reaction of the isosteric methylenephosphonate analog of alpha-D-glucose 1-phosphate with phosphoglucomutase. Induced-fit specificity revisited.
type: BibliographicResource
authors:
  item: Ray WJ Jr
  item: Post CB
  item: Puvathingal JM
journal: Biochemistry
pages: 38-47
published year: 1993
volume: 32
references: http://www.ncbi.nlm.nih.gov/pubmed/8418857

Structure of rabbit muscle phosphoglucomutase refined at 2.4-A
type: BibliographicResource
authors:
  item: Liu Y
  item: Ray WJ Jr
  item: Baranidharan S
journal: Acta Crystallogr D Biol Crystallogr
pages: 392-405
published year: 1997
volume: 53
references: http://www.ncbi.nlm.nih.gov/pubmed/15299905
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P00949
comment: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS)

Crystal structure analysis of the exocytosis-sensitive phosphoprotein, pp63/parafusin (phosphoglucomutase), from Paramecium reveals significant conformational variability.
type: BibliographicResource
authors:
  item: Muller S
  item: Diederichs K
  item: Breed J
  item: Kissmehl R
  item: Hauser K
  item: Plattner H
  item: Welte W
journal: J Mol Biol
pages: 141-53
published year: 2002
volume: 315
references: http://www.ncbi.nlm.nih.gov/pubmed/11779235
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P47244

Structural basis of diverse substrate recognition by the enzyme PMM/PGM from P. aeruginosa.
type: BibliographicResource
authors:
  item: Regni C
  item: Naught L
  item: Tipton PA
  item: Beamer LJ
journal: Structure (Camb)
pages: 55-63
published year: 2004
volume: 12
references: http://www.ncbi.nlm.nih.gov/pubmed/14725765

Cobalt (II) and nickel (II) complexes of phosphoglucomutase.
type: BibliographicResource
authors:
  item: Ray WJ Jr
  item: Goodin DS
  item: Ng L
journal: Biochemistry
pages: 2800-4
published year: 1972
volume: 11
references: http://www.ncbi.nlm.nih.gov/pubmed/5041899

Mechanism of action of rabbit muscle phosphoglucomutase. Rate of enzyme phosphate turnover studied with a rapid mixing technique.
type: BibliographicResource
authors:
  item: Walinder O
  item: Joshi JG
journal: J Biol Chem
pages: 3166-9
published year: 1974
volume: 249
references: http://www.ncbi.nlm.nih.gov/pubmed/4830239

The structure determination of rabbit phosphoglucomutase.
type: BibliographicResource
authors:
  item: Wierenga RK
  item: Lewis DG
  item: Rossmann MG
  item: Ray WJ Jr
journal: Philos Trans R Soc Lond B Biol Sci
pages: 205-8
published year: 1981
volume: 293
references: http://www.ncbi.nlm.nih.gov/pubmed/6115419

The structure of rabbit muscle phosphoglucomutase at intermediate resolution.
type: BibliographicResource
authors:
  item: Lin Z
  item: Konno M
  item: Abad-Zapatero C
  item: Wierenga R
  item: Murthy MR
  item: Ray WJ Jr
  item: Rossmann MG
journal: J Biol Chem
pages: 264-74
published year: 1986
volume: 261
references: http://www.ncbi.nlm.nih.gov/pubmed/2934384

Mechanism-based inactivation of rabbit muscle phosphoglucomutase by nojirimycin 6-phosphate.
type: BibliographicResource
authors:
  item: Kim SC
  item: Raushel FM
journal: Biochemistry
pages: 7328-32
published year: 1988
volume: 27
references: http://www.ncbi.nlm.nih.gov/pubmed/2974722

Removal of salt from a salt-induced protein crystal without cross-linking. Preliminary examination of "desalted" crystals of phosphoglucomutase by X-ray crystallography at low temperature.
type: BibliographicResource
authors:
  item: Ray WJ Jr
  item: Bolin JT
  item: Puvathingal JM
  item: Minor W
  item: Liu YW
  item: Muchmore SW
journal: Biochemistry
pages: 6866-75
published year: 1991
volume: 30
references: http://www.ncbi.nlm.nih.gov/pubmed/1712631

Formation of substrate and transition-state analogue complexes in crystals of phosphoglucomutase after removing the crystallization salt.
type: BibliographicResource
authors:
  item: Ray WJ Jr
  item: Puvathingal JM
  item: Liu YW
journal: Biochemistry
pages: 6875-85
published year: 1991
volume: 30
references: http://www.ncbi.nlm.nih.gov/pubmed/1829964

Binding energy and catalysis: deoxyfluoro sugars as probes of hydrogen bonding in phosphoglucomutase.
type: BibliographicResource
authors:
  item: Percival MD
  item: Withers SG
journal: Biochemistry
pages: 498-505
published year: 1992
volume: 31
references: http://www.ncbi.nlm.nih.gov/pubmed/1531025

Functional diversity of the phosphoglucomutase superfamily: structural implications.
type: BibliographicResource
authors:
  item: Levin S
  item: Almo SC
  item: Satir BH
journal: Protein Eng
pages: 737-46
published year: 1999
volume: 12
references: http://www.ncbi.nlm.nih.gov/pubmed/10506283

Crystal structure of PMM/PGM: an enzyme in the biosynthetic pathway of P. aeruginosa virulence factors.
type: BibliographicResource
authors:
  item: Regni C
  item: Tipton PA
  item: Beamer LJ
journal: Structure (Camb)
pages: 269-79
published year: 2002
volume: 10
references: http://www.ncbi.nlm.nih.gov/pubmed/11839312

Roles of active site residues in Pseudomonas aeruginosa phosphomannomutase/phosphoglucomutase.
type: BibliographicResource
authors:
  item: Naught LE
  item: Regni C
  item: Beamer LJ
  item: Tipton PA
journal: Biochemistry
pages: 9946-51
published year: 2003
volume: 42
references: http://www.ncbi.nlm.nih.gov/pubmed/12924943

3pmgA02
type: Pdb
catalytic residue: ARG 292
cofactor binding residue: ASP 287;ASP 289;ASP 291(Magnesium binding)
references: 3pmg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3pmg

3pmgB02
type: Pdb
catalytic residue: ARG 292
cofactor binding residue: ASP 287;ASP 289;ASP 291(Magnesium binding)
references: 3pmg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3pmg

1c47A01
type: Pdb
catalytic residue: ARG 22;SER 116;HIS 117;LYS 129
cofactor binding residue: SER 116(Magnesium binding)
references: 1c47
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1c47

1c47A02
type: Pdb
catalytic residue: ARG 292
cofactor binding residue: ASP 287;ASP 289;ASP 291(Magnesium binding)
references: 1c47
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1c47

1c47A03
type: Pdb
catalytic residue: LYS 388
references: 1c47
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1c47

1c47B01
type: Pdb
catalytic residue: ARG 22;SER 116;HIS 117;LYS 129
cofactor binding residue: SER 116(Magnesium binding)
references: 1c47
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1c47

1c47B02
type: Pdb
catalytic residue: ARG 292
cofactor binding residue: ASP 287;ASP 289;ASP 291(Magnesium binding)
references: 1c47
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1c47

1c47B03
type: Pdb
catalytic residue: LYS 388
references: 1c47
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1c47

1c4gA01
type: Pdb
catalytic residue: ARG 22;SER 116;HIS 117;LYS 129
cofactor binding residue: SER 116(Magnesium binding)
references: 1c4g
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1c4g

1c4gA02
type: Pdb
catalytic residue: ARG 292
cofactor binding residue: ASP 287;ASP 289;ASP 291(Magnesium binding)
references: 1c4g
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1c4g

1c4gA03
type: Pdb
catalytic residue: LYS 388
references: 1c4g
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1c4g

1c4gB01
type: Pdb
catalytic residue: ARG 22;SER 116;HIS 117;LYS 129
cofactor binding residue: SER 116(Magnesium binding)
references: 1c4g
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1c4g

1c4gB02
type: Pdb
catalytic residue: ARG 292
cofactor binding residue: ASP 287;ASP 289;ASP 291(Magnesium binding)
references: 1c4g
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1c4g

1c4gB03
type: Pdb
catalytic residue: LYS 388
references: 1c4g
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1c4g

1jdyA01
type: Pdb
catalytic residue: ARG 22; ;HIS 117;LYS 129
cofactor binding residue: SEP 116(Magnesium binding)
modified residue: SEP 116(Phosphonoserine)
references: 1jdy
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1jdy

1jdyA02
type: Pdb
catalytic residue: ARG 292
cofactor binding residue: ASP 287;ASP 289;ASP 291(Magnesium binding)
references: 1jdy
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1jdy

1jdyA03
type: Pdb
catalytic residue: LYS 388
references: 1jdy
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1jdy

1jdyB01
type: Pdb
catalytic residue: ARG 22; ;HIS 117;LYS 129
cofactor binding residue: SEP 116(Magnesium binding)
modified residue: SEP 116(Phosphonoserine)
references: 1jdy
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1jdy

1jdyB02
type: Pdb
catalytic residue: ARG 292
cofactor binding residue: ASP 287;ASP 289;ASP 291(Magnesium binding)
references: 1jdy
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1jdy

1jdyB03
type: Pdb
catalytic residue: LYS 388
references: 1jdy
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1jdy

1kfiA01
type: Pdb
catalytic residue: ARG 27;SER 126;HIS 127;LYS 140
cofactor binding residue: SER 126(Magnesium binding)
modified residue: SER 126(Phosphorylation)
references: 1kfi
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kfi

1kfiA02
type: Pdb
catalytic residue: ARG 313
cofactor binding residue: ASP 308;ASP 310;ASP 312(Magnesium binding)
references: 1kfi
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kfi

1kfiA03
type: Pdb
catalytic residue: LYS 405
references: 1kfi
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kfi

1kfiB01
type: Pdb
catalytic residue: ARG 27;SER 126;HIS 127;LYS 140
cofactor binding residue: SER 126(Magnesium binding)
modified residue: SER 126(Phosphorylation)
references: 1kfi
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kfi

1kfiB02
type: Pdb
catalytic residue: ARG 313
cofactor binding residue: ASP 308;ASP 310;ASP 312(Magnesium binding)
references: 1kfi
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kfi

1kfiB03
type: Pdb
catalytic residue: LYS 405
references: 1kfi
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kfi

1kfqA01
type: Pdb
catalytic residue: ARG 27;SER 126;HIS 127;LYS 140
cofactor binding residue: SER 126(Magnesium binding)
modified residue: SER 126(Phosphorylation)
references: 1kfq
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kfq

1kfqA02
type: Pdb
catalytic residue: ARG 313
cofactor binding residue: ASP 308;ASP 310;ASP 312(Magnesium binding)
references: 1kfq
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kfq

1kfqA03
type: Pdb
catalytic residue: LYS 405
references: 1kfq
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kfq

1kfqB01
type: Pdb
catalytic residue: ARG 27;SER 126;HIS 127;LYS 140
cofactor binding residue: SER 126(Magnesium binding)
modified residue: SER 126(Phosphorylation)
references: 1kfq
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kfq

1kfqB02
type: Pdb
catalytic residue: ARG 313
cofactor binding residue: ASP 308;ASP 310;ASP 312(Magnesium binding)
references: 1kfq
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kfq

1kfqB03
type: Pdb
catalytic residue: LYS 405
references: 1kfq
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kfq

1lxtA01
type: Pdb
catalytic residue: ARG 22;SER 116;HIS 117;LYS 129
cofactor binding residue: SER 116(Magnesium binding)
references: 1lxt
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1lxt

1lxtA02
type: Pdb
catalytic residue: ARG 292
cofactor binding residue: ASP 287;ASP 289;ASP 291(Magnesium binding)
references: 1lxt
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1lxt

1lxtA03
type: Pdb
catalytic residue: LYS 388
references: 1lxt
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1lxt

1lxtB01
type: Pdb
catalytic residue: ARG 22;SER 116;HIS 117;LYS 129
cofactor binding residue: SER 116(Magnesium binding)
references: 1lxt
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1lxt

1lxtB02
type: Pdb
catalytic residue: ARG 292
cofactor binding residue: ASP 287;ASP 289;ASP 291(Magnesium binding)
references: 1lxt
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1lxt

1lxtB03
type: Pdb
catalytic residue: LYS 388
references: 1lxt
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1lxt

1vklA01
type: Pdb
catalytic residue: ARG 22; ;HIS 117;LYS 129
cofactor binding residue: SER 116(Magnesium binding)
modified residue: SEP 116(Phosphonoserine)
references: 1vkl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1vkl

1vklA02
type: Pdb
catalytic residue: ARG 292
cofactor binding residue: ASP 287;ASP 289;ASP 291(Magnesium binding)
references: 1vkl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1vkl

1vklA03
type: Pdb
catalytic residue: LYS 388
references: 1vkl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1vkl

1vklB01
type: Pdb
catalytic residue: ARG 22; ;HIS 117;LYS 129
cofactor binding residue: SER 116(Magnesium binding)
modified residue: SEP 116(Phosphonoserine)
references: 1vkl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1vkl

1vklB02
type: Pdb
catalytic residue: ARG 292
cofactor binding residue: ASP 287;ASP 289;ASP 291(Magnesium binding)
references: 1vkl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1vkl

1vklB03
type: Pdb
catalytic residue: LYS 388
references: 1vkl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1vkl

2pmgA01
type: Pdb
catalytic residue: ARG 22;SER 116;HIS 117;LYS 129
cofactor binding residue: SER 116(Magnesium binding)
references: 2pmg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2pmg

2pmgA02
type: Pdb
catalytic residue: ARG 292
cofactor binding residue: ASP 287;ASP 289;ASP 291(Magnesium binding)
references: 2pmg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2pmg

2pmgA03
type: Pdb
catalytic residue: LYS 388
references: 2pmg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2pmg

2pmgB01
type: Pdb
catalytic residue: ARG 22;SER 116;HIS 117;LYS 129
cofactor binding residue: SER 116(Magnesium binding)
references: 2pmg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2pmg

2pmgB02
type: Pdb
catalytic residue: ARG 292
cofactor binding residue: ASP 287;ASP 289;ASP 291(Magnesium binding)
references: 2pmg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2pmg

2pmgB03
type: Pdb
catalytic residue: LYS 388
references: 2pmg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2pmg

3pmgA01
type: Pdb
catalytic residue: ARG 22;SER 116;HIS 117;LYS 129
cofactor binding residue: SER 116(Magnesium binding)
modified residue: SEP 116(Phosphorylation)
references: 3pmg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3pmg

3pmgA03
type: Pdb
catalytic residue: LYS 388
references: 3pmg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3pmg

3pmgB01
type: Pdb
catalytic residue: ARG 22;SER 116;HIS 117;LYS 129
cofactor binding residue: SER 116(Magnesium binding)
modified residue: SEP 116(Phosphorylation)
references: 3pmg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3pmg

3pmgB03
type: Pdb
catalytic residue: LYS 388
references: 3pmg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3pmg

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

alpha-D-Glucose 1-phosphate
type: KeggSubstrate
compound type: carbohydrate
compound type: phosphate group/phosphate ion
references: KEGG:C00103
references: CHEBI:29042
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

alpha-D-Ribose 1-phosphate
type: KeggSubstrate
compound type: carbohydrate
compound type: phosphate group/phosphate ion
references: KEGG:C00620
references: CHEBI:16300
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

D-Glucose 1,6-bisphosphate
type: KeggIntermediate
references: KEGG:C00660

alpha-D-Glucose 6-phosphate
type: KeggProduct
compound type: carbohydrate
compound type: phosphate group/phosphate ion
references: KEGG:C00668
references: CHEBI:17665
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

alpha-D-Hexose 1-phosphate
type: KeggSubstrate
compound type: carbohydrate
compound type: phosphate group/phosphate ion
references: KEGG:C01171
references: CHEBI:16326
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

alpha-D-Hexose 6-phosphate
type: KeggProduct
compound type: carbohydrate
compound type: phosphate group/phosphate ion
references: KEGG:C03735
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

alpha-D-Ribose 5-phosphate
type: KeggProduct
compound type: carbohydrate
compound type: phosphate group/phosphate ion
references: KEGG:C03736
references: CHEBI:18189
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

glucose phosphomutase
type: KeggEnzyme

phosphoglucose mutase
type: KeggEnzyme