Structure of PDB 3h3f Chain H

Receptor sequence
>3h3fH (length=331) Species: 9986 (Oryctolagus cuniculus) [Search protein sequence]
AALKDQLIHNLLKEEHVPQNKITVVGVGAVGMACAISILMKDLADELALV
DVMEDKLKGEMMDLQHGSLFLRTPKIVSGKDYSVTANSKLVIITAGARQQ
EGESRLNLVQRNVNIFKFIIPNVVKYSPHCKLLVVSNPVDILTYVAWKIS
GFPKNRVIGSGCNLDSARFRYLMGERLGVHALSCHGWILGEHGDSSVPVW
SGMNVAGVSLKTLHPELGTDADKEQWKQVHKQVVDSAYEVIKLKGYTTWA
IGLSVADLAESIMKNLRRVHPISTMLKGLYGIKEDVFLSVPCVLGQNGIS
DVVKVTLTSEEEAHLKKSADTLWGIQKELQF
3D structure
PDB3h3f Modeling of isotope effects on binding oxamate to lactic dehydrogenase
ChainH
Resolution2.38 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R105 D165 R168 H192
Catalytic site (residue number reindexed from 1) R105 D165 R168 H192
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 NAI H G28 V30 D51 V52 T94 A95 I115 V135 N137 H192 G28 V30 D51 V52 T94 A95 I115 V135 N137 H192
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:3h3f, PDBe:3h3f, PDBj:3h3f
PDBsum3h3f
PubMed19715328
UniProtP13491|LDHA_RABIT L-lactate dehydrogenase A chain (Gene Name=LDHA)

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