D00005
type: Enzyme
active site residues resources: Lactate dehydrogenase from the hyperthermophilic bacterium thermotoga maritima: the crystal structure at 2.1 A resolution reveals strategies for intrinsic protein stabilization.
active site residues resources: Q27743
active site residues resources: P00336
active site residues resources: P00339
active site residues resources: P00341
active site residues resources: P00342
active site residues resources: P00344
active site residues resources: P00343
active site residues resources: P16115
cath: Rossmann fold
cath: L-2-Hydroxyisocaproate Dehydrogenase; Chain A, domain 2
csa: 1ldm
ec: https://purl.uniprot.org/enzyme/1.1.1.27
kegg enzyme: L-lactate dehydrogenase
kegg pathway: Glycolysis / Gluconeogenesis
kegg pathway: Cysteine metabolism
kegg pathway: Pyruvate metabolism
kegg pathway: Propanoate metabolism
kegg product: Pyruvate
kegg product: NADH
kegg product: H+
kegg substrate: (S)-Lactate
kegg substrate: NAD+
pdb: 1ldbA01
pdb: 1ldnA01
pdb: 1ldnB01
pdb: 1ldnC01
pdb: 1ldnD01
pdb: 1ldnE01
pdb: 1ldnF01
pdb: 1ldnG01
pdb: 1ldnH01
pdb: 2ldbA01
pdb: 1llcA01
pdb: 1a5zA01
pdb: 1lldA01
pdb: 1lldB01
pdb: 1lthR01
pdb: 1lthT01
pdb: 1ceqA01
pdb: 1cetA01
pdb: 1ldgA01
pdb: 1t24A01
pdb: 1t25A01
pdb: 1t26A01
pdb: 1t2cA01
pdb: 1t2dA01
pdb: 1t2eA01
pdb: 1u4oA01
pdb: 1u4sA01
pdb: 1u5aA01
pdb: 1u5cA01
pdb: 1xivA01
pdb: 2a94A01
pdb: 1ldmA01
pdb: 3ldhA01
pdb: 6ldhA01
pdb: 8ldhA01
pdb: 9ldbA01
pdb: 9ldbB01
pdb: 9ldtA01
pdb: 9ldtB01
pdb: 5ldhA01
pdb: 2ldxA01
pdb: 1i10A01
pdb: 1i10B01
pdb: 1i10C01
pdb: 1i10D01
pdb: 1i10E01
pdb: 1i10F01
pdb: 1i10G01
pdb: 1i10H01
pdb: 1i0zA01
pdb: 1i0zB01
pdb: 1t2fA01
pdb: 1t2fB01
pdb: 1t2fC01
pdb: 1t2fD01
pdb: 1ldbA02

Analogue
compound: (S)-Lactate
ligand het code: CIT_1
pdb: 8ldhA02

Analogue
compound: (S)-Lactate
ligand het code: LNC(S-lactate)
pdb: 5ldhA02

Analogue
compound: NAD+
ligand het code: LNC(NAD)
pdb: 5ldhA01

Analogue
compound: Pyruvate
ligand het code: OXM
pdb: 1ldnA02

Analogue
compound: Pyruvate
ligand het code: OXM
pdb: 1ldnB02

Analogue
compound: Pyruvate
ligand het code: OXM
pdb: 1ldnC02

Analogue
compound: Pyruvate
ligand het code: OXM
pdb: 1ldnD02

Analogue
compound: Pyruvate
ligand het code: OXM
pdb: 1ldnE02

Analogue
compound: Pyruvate
ligand het code: OXM
pdb: 1ldnF02

Analogue
compound: Pyruvate
ligand het code: OXM
pdb: 1ldnG02

Analogue
compound: Pyruvate
ligand het code: OXM
pdb: 1ldnH02

Analogue
compound: Pyruvate
ligand het code: OXM
pdb: 1a5zA02

Analogue
compound: Pyruvate
ligand het code: OXM
pdb: 1lthR02

Analogue
compound: Pyruvate
ligand het code: OXM
pdb: 1ldgA02

Analogue
compound: Pyruvate
ligand het code: OXQ
pdb: 1t24A02

Analogue
compound: Pyruvate
ligand het code: GAG
pdb: 1t25A02

Analogue
compound: Pyruvate
ligand het code: GBD
pdb: 1t26A02

Analogue
compound: Pyruvate
ligand het code: OXL
pdb: 1t2dA02

Analogue
compound: Pyruvate
ligand het code: OXM
pdb: 1t2eA02

Analogue
compound: Pyruvate
ligand het code: BIK
pdb: 1u5aA02

Analogue
compound: Pyruvate
ligand het code: BIK
pdb: 1u5cA02

Analogue
compound: Pyruvate
ligand het code: OXM
pdb: 1ldmA02

Analogue
compound: Pyruvate
ligand het code: OXM
pdb: 9ldbB02

Analogue
compound: Pyruvate
ligand het code: OXM
pdb: 9ldtA02

Analogue
compound: Pyruvate
ligand het code: OXM
pdb: 9ldtB02

Analogue
compound: Pyruvate
ligand het code: OXM
pdb: 1i10A02

Analogue
compound: Pyruvate
ligand het code: OXM
pdb: 1i10B02

Analogue
compound: Pyruvate
ligand het code: OXM
pdb: 1i10C02

Analogue
compound: Pyruvate
ligand het code: OXM
pdb: 1i10D02

Analogue
compound: Pyruvate
ligand het code: OXM
pdb: 1i10E02

Analogue
compound: Pyruvate
ligand het code: OXM
pdb: 1i10F02

Analogue
compound: Pyruvate
ligand het code: OXM
pdb: 1i10G02

Analogue
compound: Pyruvate
ligand het code: OXM
pdb: 1i10H02

Analogue
compound: Pyruvate
ligand het code: OXM
pdb: 1i0zA02

Analogue
compound: Pyruvate
ligand het code: OXM
pdb: 1i0zB02

Analogue
compound: Pyruvate
ligand het code: OXQ
pdb: 1t2fA02

Analogue
compound: Pyruvate
ligand het code: OXQ
pdb: 1t2fB02

Analogue
compound: Pyruvate
ligand het code: OXQ
pdb: 1t2fC02

Analogue
compound: Pyruvate
ligand het code: OXQ
pdb: 1t2fD02

Analogue
compound: NADH
ligand het code: AP0
pdb: 2a94A01

ReferenceForCatalyticMechanism
reference index: 3
reference section: Fig.2, p.2677-2679

ReferenceForCatalyticMechanism
reference index: 5
reference section: Fig.9, p.303-305

ReferenceForCatalyticMechanism
reference index: 9
reference section: p.462-465

ReferenceForCatalyticMechanism
reference index: 12
reference section: Fig.1, p.178-179

ReferenceForCatalyticMechanism
reference index: 16
reference section: Fig.12, p.1133-1137

ReferenceForCatalyticMechanism
reference index: 22
reference section: Fig. 1, p.228

ReferenceForCatalyticMechanism
reference index: 23
reference section: p.771

ReferenceForCatalyticMechanism
reference index: 28
reference section: p.1355-1358

Rossmann fold
type: Cath
catalytic domain: index.html
references: http://www.cathdb.info/version/latest/superfamily/3.40.50.720

L-2-Hydroxyisocaproate Dehydrogenase; Chain A, domain 2
type: Cath
catalytic domain: index.html
references: http://www.cathdb.info/version/latest/superfamily/3.90.110.10

H+
type: KeggProduct
compound type: others
references: KEGG:C00080
references: CHEBI:15378
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Glycolysis / Gluconeogenesis
type: KeggPathway
references: KEGG:MAP00010

Cysteine metabolism
type: KeggPathway
references: KEGG:MAP00272

Pyruvate metabolism
type: KeggPathway
references: KEGG:MAP00620

Propanoate metabolism
type: KeggPathway
references: KEGG:MAP00640

Atomic co-ordinates for dogfish M4 apo-lactate dehydrogenase.
type: BibliographicResource
authors:
  item: Adams MJ
  item: Ford GC
  item: Liljas A
  item: Rossmann MG
journal: Biochem Biophys Res Commun
pages: 46-51
published year: 1973
volume: 53
references: http://www.ncbi.nlm.nih.gov/pubmed/4795361
references: P00341
comment: ATOMIC COORDINATES

D-lactate dehydrogenase. Substrate specificity and use as a catalyst in the synthesis of homochiral 2-hydroxy acids.
type: BibliographicResource
authors:
  item: Simon ES
  item: Plante R
  item: Whitesides GM
journal: Appl Biochem Biotechnol
pages: 169-79
published year: 1989
volume: 22
references: http://www.ncbi.nlm.nih.gov/pubmed/2610514

Structure determination and refinement of Bacillus stearothermophilus lactate dehydrogenase.
type: BibliographicResource
authors:
  item: Piontek K
  item: Chakrabarti P
  item: Schar HP
  item: Rossmann MG
  item: Zuber H
journal: Proteins
pages: 74-92
published year: 1990
volume: 7
references: http://www.ncbi.nlm.nih.gov/pubmed/2330370
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

Design and synthesis of new enzymes based on the lactate dehydrogenase framework.
type: BibliographicResource
authors:
  item: Dunn CR
  item: Wilks HM
  item: Halsall DJ
  item: Atkinson T
  item: Clarke AR
  item: Muirhead H
  item: Holbrook JJ
journal: Philos Trans R Soc Lond B Biol Sci
pages: 177-84
published year: 1991
volume: 332
references: http://www.ncbi.nlm.nih.gov/pubmed/1678537
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P00339
comment: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS)

Structure of a ternary complex of an allosteric lactate dehydrogenase from Bacillus stearothermophilus at 2.5 A resolution.
type: BibliographicResource
authors:
  item: Wigley DB
  item: Gamblin SJ
  item: Turkenburg JP
  item: Dodson EJ
  item: Piontek K
  item: Muirhead H
  item: Holbrook JJ
journal: J Mol Biol
pages: 317-35
published year: 1992
volume: 223
references: http://www.ncbi.nlm.nih.gov/pubmed/1731077
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P00344
comment: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS)

Charge balance in the alpha-hydroxyacid dehydrogenase vacuole: an acid test.
type: BibliographicResource
authors:
  item: Cortes A
  item: Emery DC
  item: Halsall DJ
  item: Jackson RM
  item: Clarke AR
  item: Holbrook JJ
journal: Protein Sci
pages: 892-901
published year: 1992
volume: 1
references: http://www.ncbi.nlm.nih.gov/pubmed/1304374

Molecular basis of allosteric activation of bacterial L-lactate dehydrogenase.
type: BibliographicResource
authors:
  item: Iwata S
  item: Ohta T
journal: J Mol Biol
pages: 21-7
published year: 1993
volume: 230
references: http://www.ncbi.nlm.nih.gov/pubmed/8450537
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P19869
comment: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS)

Crystal structure of a NAD-dependent D-glycerate dehydrogenase at 2.4 A resolution.
type: BibliographicResource
authors:
  item: Goldberg JD
  item: Yoshida T
  item: Brick P
journal: J Mol Biol
pages: 236(4)
published year: 1994
volume: 1123-4
references: http://www.ncbi.nlm.nih.gov/pubmed/8120891

T and R states in the crystals of bacterial L-lactate dehydrogenase reveal the mechanism for allosteric control.
type: BibliographicResource
authors:
  item: Iwata S
  item: Kamata K
  item: Yoshida S
  item: Minowa T
  item: Ohta T
journal: Nat Struct Biol
pages: 176-85
published year: 1994
volume: 1
references: http://www.ncbi.nlm.nih.gov/pubmed/7656036
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P19869
comment: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS)

Identifying the mechanism of protein loop closure: a molecular dynamics simulation of the Bacillus stearothermophilus LDH loop in solution.
type: BibliographicResource
authors:
  item: Philippopoulos M
  item: Xiang Y
  item: Lim C
journal: Protein Eng
pages: 565-73
published year: 1995
volume: 8
references: http://www.ncbi.nlm.nih.gov/pubmed/8532681

The structure of lactate dehydrogenase from Plasmodium falciparum reveals a new target for anti-malarial design.
type: BibliographicResource
authors:
  item: Dunn CR
  item: Banfield MJ
  item: Barker JJ
  item: Higham CW
  item: Moreton KM
  item: Turgut-Balik D
  item: Brady RL
  item: Holbrook JJ
journal: Nat Struct Biol
pages: 912-5
published year: 1996
volume: 3
references: http://www.ncbi.nlm.nih.gov/pubmed/8901865
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: Q27743
comment: X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS)

A comparison of the structures of apo dogfish M4 lactate dehydrogenase and its ternary complexes.
type: BibliographicResource
authors:
  item: White JL
  item: Hackert ML
  item: Buehner M
  item: Adams MJ
  item: Ford GC
  item: Lentz PJ Jr
  item: Smiley IE
  item: Steindel SJ
  item: Rossmann MG
journal: J Mol Biol
pages: 759-79
published year: 1976
volume: 102
references: http://www.ncbi.nlm.nih.gov/pubmed/940154
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

Molecular dynamics simulations of N-terminal peptides from a nucleotide binding protein.
type: BibliographicResource
authors:
  item: van der Spoel D
  item: Vogel HJ
  item: Berendsen HJ
journal: Proteins
pages: 450-66
published year: 1996
volume: 24
references: http://www.ncbi.nlm.nih.gov/pubmed/9162946

The contribution of electrostatic and van der Waals interactions to the stereospecificity of the reaction catalyzed by lactate dehydrogenase.
type: BibliographicResource
authors:
  item: van Beek J
  item: Callender R
  item: Gunner MR
journal: Biophys J
pages: 619-26
published year: 1997
volume: 72
references: http://www.ncbi.nlm.nih.gov/pubmed/9017191

Correlation of the enzyme activities of Bacillus stearothermophilus lactate dehydrogenase on three substrates with the results of molecular dynamics/energy minimization conformational searching.
type: BibliographicResource
authors:
  item: Dafforn TR
  item: Badcoe IG
  item: Sessions RB
  item: el Hawrani AS
  item: Holbrook JJ
journal: Proteins
pages: 228-39
published year: 1997
volume: 29
references: http://www.ncbi.nlm.nih.gov/pubmed/9329087

Chloroquine binds in the cofactor binding site of Plasmodium falciparum lactate dehydrogenase.
type: BibliographicResource
authors:
  item: Read JA
  item: Wilkinson KW
  item: Tranter R
  item: Sessions RB
  item: Brady RL
journal: J Biol Chem
pages: 10213-8
published year: 1999
volume: 274
references: http://www.ncbi.nlm.nih.gov/pubmed/10187806
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

Redesign of the coenzyme specificity in L-lactate dehydrogenase from bacillus stearothermophilus using site-directed mutagenesis and media engineering.
type: BibliographicResource
authors:
  item: Holmberg N
  item: Ryde U
  item: Bulow L
journal: Protein Eng
pages: 851-6
published year: 1999
volume: 12
references: http://www.ncbi.nlm.nih.gov/pubmed/10556245

epsilon-crystallin from duck eye lens comparison of its quaternary structure and stability with other lactate dehydrogenases and complex formation with alpha-crystallin.
type: BibliographicResource
authors:
  item: Berr K
  item: Wassenberg D
  item: Lilie H
  item: Behlke J
  item: Jaenicke R
journal: Eur J Biochem
pages: 5413-20
published year: 2000
volume: 267
references: http://www.ncbi.nlm.nih.gov/pubmed/10951199

The A245K mutation exposes another stage of the bacterial L-lactate dehydrogenase reaction mechanism.
type: BibliographicResource
authors:
  item: Kedzierski P
  item: Moreton K
  item: Clarke AR
  item: Holbrook JJ
journal: Biochemistry
pages: 7247-52
published year: 2001
volume: 40
references: http://www.ncbi.nlm.nih.gov/pubmed/11401572

Crystal structure of the MJ0490 gene product of the hyperthermophilic archaebacterium Methanococcus jannaschii, a novel member of the lactate/malate family of dehydrogenases.
type: BibliographicResource
authors:
  item: Lee BI
  item: Chang C
  item: Cho SJ
  item: Eom SH
  item: Kim KK
  item: Yu YG
  item: Suh SW
journal: J Mol Biol
pages: 1351-62
published year: 2001
volume: 307
references: http://www.ncbi.nlm.nih.gov/pubmed/11292347

Structural basis for altered activity of M- and H-isozyme forms of human lactate dehydrogenase.
type: BibliographicResource
authors:
  item: Read JA
  item: Winter VJ
  item: Eszes CM
  item: Sessions RB
  item: Brady RL
journal: Proteins
pages: 175-85
published year: 2001
volume: 43
references: http://www.ncbi.nlm.nih.gov/pubmed/11276087
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

Structural adaptations of lactate dehydrogenase isozymes.
type: BibliographicResource
authors:
  item: Eventoff W
  item: Rossmann MG
  item: Taylor SS
  item: Torff HJ
  item: Meyer H
  item: Keil W
  item: Kiltz HH
journal: Proc Natl Acad Sci U S A
pages: 2677-81
published year: 1977
volume: 74
references: http://www.ncbi.nlm.nih.gov/pubmed/197516
references: P00341
comment: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS)

Crystal structure of non-allosteric L-lactate dehydrogenase from Lactobacillus pentosus at 2.3 A resolution: specific interactions at subunit interfaces.
type: BibliographicResource
authors:
  item: Uchikoba H
  item: Fushinobu S
  item: Wakagi T
  item: Konno M
  item: Taguchi H
  item: Matsuzawa H
journal: Proteins
pages: 206-14
published year: 2002
volume: 46
references: http://www.ncbi.nlm.nih.gov/pubmed/11807949

Crystal structure of Plasmodium berghei lactate dehydrogenase indicates the unique structural differences of these enzymes are shared across the Plasmodium genus.
type: BibliographicResource
authors:
  item: Winter VJ
  item: Cameron A
  item: Tranter R
  item: Sessions RB
  item: Brady RL
journal: Mol Biochem Parasitol
pages: 1-10
published year: 2003
volume: 131
references: http://www.ncbi.nlm.nih.gov/pubmed/12967707

Comparative structural analysis and kinetic properties of lactate dehydrogenases from the four species of human malarial parasites.
type: BibliographicResource
authors:
  item: Brown WM
  item: Makler MT
  item: Vander Jagt DL
  item: Yowell CA
  item: Hoard A
  item: Vander Jagt TA
  item: Hunsaker LA
  item: Deck LM
  item: Royer RE
  item: Piper RC
  item: Dame JB
journal: Biochemistry
pages: 6219-29
published year: 2004
volume: 43
references: http://www.ncbi.nlm.nih.gov/pubmed/15147206

Identification and activity of a series of azole-based compounds with lactate dehydrogenase-directed anti-malarial activity.
type: BibliographicResource
authors:
  item: Cameron A
  item: Croft SL
  item: Barros D
  item: Lavandera JL
  item: Martin JJ
  item: Risco F
  item: Garcia-Ochoa S
  item: Gamo FJ
  item: Sanz L
  item: Leon L
  item: Ruiz JR
  item: Read J
  item: Gabarro R
  item: Mallo A
  item: Gomez de las Heras F
  item: Tranter R
  item: Winter VJ
  item: Sessions RB
  item: Brady RL
  item: Vivas L
  item: Easton A
  item: Kendrick H
journal: J Biol Chem
pages: 31429-39
published year: 2004
volume: 279
references: http://www.ncbi.nlm.nih.gov/pubmed/15117937
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Mapping the binding site for gossypol-like inhibitors of Plasmodium falciparum lactate dehydrogenase.
type: BibliographicResource
authors:
  item: Conners R
  item: Schambach F
  item: Read J
  item: Cameron A
  item: Sessions RB
  item: Vivas L
  item: Easton A
  item: Croft SL
  item: Brady RL
journal: Mol Biochem Parasitol
pages: 137-48
published year: 2005
volume: 142
references: http://www.ncbi.nlm.nih.gov/pubmed/15978953
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Structure of lactate dehydrogenase from Plasmodium vivax: complexes with NADH and APADH.
type: BibliographicResource
authors:
  item: Chaikuad A
  item: Fairweather V
  item: Conners R
  item: Joseph-Horne T
  item: Turgut-Balik D
  item: Brady RL
journal: Biochemistry
pages: 16221-8
published year: 2005
volume: 44
references: http://www.ncbi.nlm.nih.gov/pubmed/16331982
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

The structure of mouse testicular lactate dehydrogenase isoenzyme C4 at 2.9 A resolution.
type: BibliographicResource
authors:
  item: Musick WD
  item: Rossmann MG
journal: J Biol Chem
pages: 7611-20
published year: 1979
volume: 254
references: http://www.ncbi.nlm.nih.gov/pubmed/468772
references: P00342
comment: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS)

Structure of the active ternary complex of pig heart lactate dehydrogenase with S-lac-NAD at 2.7 A resolution.
type: BibliographicResource
authors:
  item: Grau UM
  item: Trommer WE
  item: Rossmann MG
journal: J Mol Biol
pages: 289-307
published year: 1981
volume: 151
references: http://www.ncbi.nlm.nih.gov/pubmed/7338899
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P00336
comment: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS)

The complete primary structure of the allosteric L-lactate dehydrogenase from Lactobacillus casei.
type: BibliographicResource
authors:
  item: Hensel R
  item: Mayr U
  item: Yang CY
journal: Eur J Biochem
pages: 503-11
published year: 1983
volume: 134
references: http://www.ncbi.nlm.nih.gov/pubmed/6411465
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

Structure determination of the allosteric L-lactate dehydrogenase from Lactobacillus-casei at 3A resolution.
type: BibliographicResource
authors:
  item: Buehner M
  item: Hecht HJ
journal: Acta Crystallogr A
pages: 32-4
published year: 1984
volume: 40
references: P00343
comment: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).

Characterization of the antigenic sites on the refined 3-A resolution structure of mouse testicular lactate dehydrogenase C4.
type: BibliographicResource
authors:
  item: Hogrefe HH
  item: Griffith JP
  item: Rossmann MG
  item: Goldberg E
journal: J Biol Chem
pages: 13155-62
published year: 1987
volume: 262
references: http://www.ncbi.nlm.nih.gov/pubmed/2443489
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography

Refined crystal structure of dogfish M4 apo-lactate dehydrogenase.
type: BibliographicResource
authors:
  item: Abad-Zapatero C
  item: Griffith JP
  item: Sussman JL
  item: Rossmann MG
journal: J Mol Biol
pages: 445-67
published year: 1987
volume: 198
references: http://www.ncbi.nlm.nih.gov/pubmed/3430615
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P00341
comment: X-RAY CRYSTALLOGRAPHY (0.25 ANGSTROMS).

Lactate dehydrogenase from the hyperthermophilic bacterium thermotoga maritima: the crystal structure at 2.1 A resolution reveals strategies for intrinsic protein stabilization.
type: BibliographicResource
authors:
  item: Auerbach G
  item: Ostendorp R
  item: Prade L
  item: Korndorfer I
  item: Dams T
  item: Huber R
  item: Jaenicke R
journal: Structure
pages: 769-81
published year: 1998
volume: 6
references: http://www.ncbi.nlm.nih.gov/pubmed/9655830
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P16115
comment: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS)

1a5zA01
type: Pdb
catalytic residue: ARG 109
references: 1a5z
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1a5z

1i0zA01
type: Pdb
catalytic residue: ARG 106
references: 1i0z
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1i0z

1i0zB01
type: Pdb
catalytic residue: ARG 106
references: 1i0z
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1i0z

1i10A01
type: Pdb
catalytic residue: ARG 105
references: 1i10
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1i10

1i10B01
type: Pdb
catalytic residue: ARG 105
references: 1i10
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1i10

1i10C01
type: Pdb
catalytic residue: ARG 105
references: 1i10
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1i10

1i10D01
type: Pdb
catalytic residue: ARG 105
references: 1i10
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1i10

1i10E01
type: Pdb
catalytic residue: ARG 105
references: 1i10
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1i10

1i10F01
type: Pdb
catalytic residue: ARG 105
references: 1i10
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1i10

1i10G01
type: Pdb
references: 1i10
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1i10
comment: invisible 101-106

1i10H01
type: Pdb
catalytic residue: ARG 105
references: 1i10
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1i10

1ldgA01
type: Pdb
catalytic residue: ARG 109
references: 1ldg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ldg

1ldmA01
type: Pdb
catalytic residue: ARG 106
references: 1ldm
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ldm

1ldnA01
type: Pdb
catalytic residue: ARG 106
references: 1ldn
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ldn

1ldnB01
type: Pdb
catalytic residue: ARG 106
references: 1ldn
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ldn

1ldnC01
type: Pdb
catalytic residue: ARG 106
references: 1ldn
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ldn

1ldnD01
type: Pdb
catalytic residue: ARG 106
references: 1ldn
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ldn

1ldnE01
type: Pdb
catalytic residue: ARG 106
references: 1ldn
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ldn

1ldnF01
type: Pdb
catalytic residue: ARG 106
references: 1ldn
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ldn

1ldnG01
type: Pdb
catalytic residue: ARG 106
references: 1ldn
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ldn

1ldnH01
type: Pdb
catalytic residue: ARG 106
references: 1ldn
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ldn

1lldA01
type: Pdb
catalytic residue: ARG 93
references: 1lld
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1lld

1lldB01
type: Pdb
catalytic residue: ARG 93
references: 1lld
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1lld

1lthR01
type: Pdb
catalytic residue: ARG 93
references: 1lth
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1lth

1lthT01
type: Pdb
catalytic residue: ARG 93
references: 1lth
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1lth

1t24A01
type: Pdb
catalytic residue: ARG 109
references: 1t24
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1t24

1t25A01
type: Pdb
catalytic residue: ARG 109
references: 1t25
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1t25

1t26A01
type: Pdb
catalytic residue: ARG 109
references: 1t26
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1t26

1t2cA01
type: Pdb
catalytic residue: ARG 109
references: 1t2c
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1t2c

1t2dA01
type: Pdb
catalytic residue: ARG 94
references: 1t2d
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1t2d

1t2eA01
type: Pdb
catalytic residue: ARG 109
references: 1t2e
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1t2e

1t2fA01
type: Pdb
catalytic residue: ARG 106
references: 1t2f
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1t2f

1t2fB01
type: Pdb
catalytic residue: ARG 106
references: 1t2f
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1t2f

1t2fC01
type: Pdb
catalytic residue: ARG 106
references: 1t2f
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1t2f

1t2fD01
type: Pdb
catalytic residue: ARG 106
references: 1t2f
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1t2f

1u5cA01
type: Pdb
catalytic residue: ARG 109
references: 1u5c
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1u5c

2ldbA01
type: Pdb
references: 2ldb
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2ldb
comment: invisible 99-106

3ldhA01
type: Pdb
catalytic residue: ARG 109
references: 3ldh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3ldh

3ldhA02
type: Pdb
catalytic residue: ASP 168;ARG 171;HIS 195
references: 3ldh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3ldh

9ldbA01
type: Pdb
catalytic residue: ARG 109
references: 9ldb
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:9ldb

9ldbB01
type: Pdb
catalytic residue: ARG 109
references: 9ldb
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:9ldb

9ldtA01
type: Pdb
catalytic residue: ARG 109
references: 9ldt
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:9ldt

9ldtB01
type: Pdb
catalytic residue: ARG 109
references: 9ldt
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:9ldt

1a5zA02
type: Pdb
catalytic residue: ASP 168;ARG 171;HIS 195
references: 1a5z
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1a5z

1ceqA01
type: Pdb
catalytic residue: ARG 109
references: 1ceq
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ceq

1ceqA02
type: Pdb
catalytic residue: ASP 168;ARG 171;HIS 195
references: 1ceq
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ceq

1cetA01
type: Pdb
catalytic residue: ARG 109
references: 1cet
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1cet

1cetA02
type: Pdb
catalytic residue: ASP 168;ARG 171;HIS 195
references: 1cet
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1cet

1i0zA02
type: Pdb
catalytic residue: ASP 166;ARG 169;HIS 193
references: 1i0z
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1i0z

1i0zB02
type: Pdb
catalytic residue: ASP 166;ARG 169;HIS 193
references: 1i0z
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1i0z

1i10A02
type: Pdb
catalytic residue: ASP 165;ARG 168;HIS 192
references: 1i10
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1i10

1i10B02
type: Pdb
catalytic residue: ASP 165;ARG 168;HIS 192
references: 1i10
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1i10

1i10C02
type: Pdb
catalytic residue: ASP 165;ARG 168;HIS 192
references: 1i10
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1i10

1i10D02
type: Pdb
catalytic residue: ASP 165;ARG 168;HIS 192
references: 1i10
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1i10

1i10E02
type: Pdb
catalytic residue: ASP 165;ARG 168;HIS 192
references: 1i10
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1i10

1i10F02
type: Pdb
catalytic residue: ASP 165;ARG 168;HIS 192
references: 1i10
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1i10

1i10G02
type: Pdb
catalytic residue: ASP 165;ARG 168;HIS 192
references: 1i10
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1i10

1i10H02
type: Pdb
catalytic residue: ASP 165;ARG 168;HIS 192
references: 1i10
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1i10

1ldbA01
type: Pdb
references: 1ldb
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ldb
comment: invisible 100-107

1ldbA02
type: Pdb
catalytic residue: ASP 166;ARG 169;HIS 193
references: 1ldb
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ldb

1ldgA02
type: Pdb
catalytic residue: ASP 168;ARG 171;HIS 195
references: 1ldg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ldg

1ldmA02
type: Pdb
catalytic residue: ASP 166;ARG 169;HIS 193
references: 1ldm
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ldm

1ldnA02
type: Pdb
catalytic residue: ASP 166;ARG 169;HIS 193
references: 1ldn
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ldn

1ldnB02
type: Pdb
catalytic residue: ASP 166;ARG 169;HIS 193
references: 1ldn
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ldn

1ldnC02
type: Pdb
catalytic residue: ASP 166;ARG 169;HIS 193
references: 1ldn
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ldn

1ldnD02
type: Pdb
catalytic residue: ASP 166;ARG 169;HIS 193
references: 1ldn
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ldn

1ldnE02
type: Pdb
catalytic residue: ASP 166;ARG 169;HIS 193
references: 1ldn
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ldn

1ldnF02
type: Pdb
catalytic residue: ASP 166;ARG 169;HIS 193
references: 1ldn
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ldn

1ldnG02
type: Pdb
catalytic residue: ASP 166;ARG 169;HIS 193
references: 1ldn
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ldn

1ldnH02
type: Pdb
catalytic residue: ASP 166;ARG 169;HIS 193
references: 1ldn
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1ldn

1llcA01
type: Pdb
catalytic residue: ARG 109
references: 1llc
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1llc

1llcA02
type: Pdb
catalytic residue: ASP 168;ARG 171;HIS 195
references: 1llc
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1llc

1lldA02
type: Pdb
catalytic residue: ASP 153;ARG 156;HIS 180
references: 1lld
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1lld
comment: mutant C199S

1lldB02
type: Pdb
catalytic residue: ASP 153;ARG 156;HIS 180
references: 1lld
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1lld
comment: mutant C199S

1lthR02
type: Pdb
catalytic residue: ASP 153;ARG 156;HIS 180
references: 1lth
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1lth
comment: mutant C199S

1lthT02
type: Pdb
catalytic residue: ASP 153;ARG 156;HIS 180
references: 1lth
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1lth
comment: mutant C199S

1t24A02
type: Pdb
catalytic residue: ASP 168;ARG 171;HIS 195
references: 1t24
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1t24

1t25A02
type: Pdb
catalytic residue: ASP 168;ARG 171;HIS 195
references: 1t25
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1t25

1t26A02
type: Pdb
catalytic residue: ASP 168;ARG 171;HIS 195
references: 1t26
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1t26

1t2cA02
type: Pdb
catalytic residue: ASP 168;ARG 171;HIS 195
references: 1t2c
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1t2c

1t2dA02
type: Pdb
catalytic residue: ASP 154;ARG 157;HIS 181
references: 1t2d
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1t2d

1t2eA02
type: Pdb
catalytic residue: ASP 168;ARG 171;HIS 195
references: 1t2e
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1t2e

1t2fA02
type: Pdb
catalytic residue: ASP 166;ARG 169;HIS 193
references: 1t2f
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1t2f

1t2fB02
type: Pdb
catalytic residue: ASP 166;ARG 169;HIS 193
references: 1t2f
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1t2f

1t2fC02
type: Pdb
catalytic residue: ASP 166;ARG 169;HIS 193
references: 1t2f
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1t2f

1t2fD02
type: Pdb
catalytic residue: ASP 166;ARG 169;HIS 193
references: 1t2f
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1t2f

1u4oA01
type: Pdb
catalytic residue: ARG 109
references: 1u4o
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1u4o

1u4oA02
type: Pdb
catalytic residue: ASP 168;ARG 171;HIS 195
references: 1u4o
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1u4o

1u4sA01
type: Pdb
catalytic residue: ARG 109
references: 1u4s
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1u4s

1u4sA02
type: Pdb
catalytic residue: ASP 168;ARG 171;HIS 195
references: 1u4s
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1u4s

1u5aA01
type: Pdb
catalytic residue: ARG 109
references: 1u5a
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1u5a

1u5aA02
type: Pdb
catalytic residue: ASP 168;ARG 171;HIS 195
references: 1u5a
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1u5a

1u5cA02
type: Pdb
catalytic residue: ASP 168;ARG 171;HIS 195
references: 1u5c
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1u5c

1xivA01
type: Pdb
catalytic residue: ARG 109
references: 1xiv
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1xiv

1xivA02
type: Pdb
catalytic residue: ASP 168;ARG 171;HIS 195
references: 1xiv
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1xiv

2a94A01
type: Pdb
catalytic residue: ARG 109
references: 2a94
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2a94

2a94A02
type: Pdb
catalytic residue: ASP 168;ARG 171;HIS 195
references: 2a94
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2a94

2ldbA02
type: Pdb
catalytic residue: ASP 166;ARG 169;HIS 193
references: 2ldb
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2ldb

2ldxA01
type: Pdb
catalytic residue: ARG 105
references: 2ldx
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2ldx

2ldxA02
type: Pdb
catalytic residue: ASP 165;ARG 168;HIS 192
references: 2ldx
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2ldx

5ldhA01
type: Pdb
catalytic residue: ARG 109
references: 5ldh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:5ldh

5ldhA02
type: Pdb
catalytic residue: ASP 168;ARG 171;HIS 195
references: 5ldh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:5ldh

6ldhA01
type: Pdb
catalytic residue: ARG 106
references: 6ldh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:6ldh

6ldhA02
type: Pdb
catalytic residue: ASP 166;ARG 169;HIS 193
references: 6ldh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:6ldh

8ldhA01
type: Pdb
catalytic residue: ARG 106
references: 8ldh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:8ldh

8ldhA02
type: Pdb
catalytic residue: ASP 166;ARG 169;HIS 193
references: 8ldh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:8ldh

9ldbA02
type: Pdb
catalytic residue: ASP 168;ARG 171;HIS 195
references: 9ldb
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:9ldb

9ldbB02
type: Pdb
catalytic residue: ASP 168;ARG 171;HIS 195
references: 9ldb
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:9ldb

9ldtA02
type: Pdb
catalytic residue: ASP 168;ARG 171;HIS 195
references: 9ldt
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:9ldt

9ldtB02
type: Pdb
catalytic residue: ASP 168;ARG 171;HIS 195
references: 9ldt
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:9ldt

NAD+
type: KeggSubstrate
compound type: amide group
compound type: amine group
compound type: nucleotide
references: KEGG:C00003
references: CHEBI:15846
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

NADH
type: KeggProduct
compound type: amide group
compound type: amine group
compound type: nucleotide
references: KEGG:C00004
references: CHEBI:16908
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

(S)-Lactate
type: KeggSubstrate
compound type: carbohydrate
compound type: carboxyl group
references: KEGG:C00186
references: CHEBI:422
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

lactic acid dehydrogenase
type: KeggEnzyme

L(+)-nLDH
type: KeggEnzyme

L-(+)-lactate dehydrogenase
type: KeggEnzyme

L-lactic dehydrogenase
type: KeggEnzyme

L-lactic acid dehydrogenase
type: KeggEnzyme

lactate dehydrogenase
type: KeggEnzyme

lactate dehydrogenase NAD+-dependent
type: KeggEnzyme

lactic dehydrogenase
type: KeggEnzyme

NAD+-lactate dehydrogenase
type: KeggEnzyme