Structure of PDB 1v6a Chain A

Receptor sequence
>1v6aA (length=332) Species: 7962 (Cyprinus carpio) [Search protein sequence]
ASTKEKLITHVSKEEPAGPTNKVTVVGVGMVGMAAAISILLKDLTDELAL
VDVMEDKLKGEAMDLQHGSLFLKTHKIVADKDYSVTANSKVVVVTAGARQ
QEGESRLNLVQRNVNIFKFIIPNIIKYSPNCILLVVSNPVDILTYVAWKL
SGLPRNRVIGSGTNLDSARFRHLMGEKLGIHPSNCHGWVIGEHGDSSVPV
WSGVNVAGVFLQGLNPDMGTDKDKEDWKSVHKMVVDSAYEVIKLKGYTSW
AIGMSAADLCQSILKNLRKCHPVSTLVKGMHGVNEEVFLSVPCILGNSGL
TDVVHMTLKSDEEKQLVKSAETLWGVQKDLTL
3D structure
PDB1v6a Crystal Structure of L-lactate dehydrogenase from Cyprinus carpio
ChainA
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R106 D166 R169 H193
Catalytic site (residue number reindexed from 1) R106 D166 R169 H193
Enzyme Commision number 1.1.1.27: L-lactate dehydrogenase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 GLC A E47 S84 V85 E47 S84 V85
BS02 GLC A V28 G29 D52 A96 G97 V28 G29 D52 A96 G97
BS03 GLC A G97 R99 G97 R99
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004459 L-lactate dehydrogenase activity
GO:0016491 oxidoreductase activity
GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Biological Process
GO:0006089 lactate metabolic process
GO:0006090 pyruvate metabolic process
GO:0019752 carboxylic acid metabolic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1v6a, PDBe:1v6a, PDBj:1v6a
PDBsum1v6a
PubMed
UniProtQ9W7K5|LDHA_CYPCA L-lactate dehydrogenase A chain (Gene Name=ldha)

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