Structure of PDB 4i8x Chain H

Receptor sequence
>4i8xH (length=331) Species: 9986 (Oryctolagus cuniculus) [Search protein sequence]
AALKDQLIHNLLKEEHVPQNKITVVGVGAVGMACAISILMKDLADELALV
DVMEDKLKGEMMDLQHGSLFLRTPKIVSGKDYSVTANSKLVIITAGARQQ
EGESRLNLVQRNVNIFKFIIPNVVKYSPHCKLLVVSNPVDILTYVAWKIS
GFPKNRVIGSGCNLDSARFRYLMGERLGVHALSCHGWILGEHGDSSVPVW
SGMNVAGVSLKTLHPELGTDADKEQWKQVHKQVVDSAYEVIKLKGYTTWA
IGLSVADLAESIMKNLRRVHPISTMLKGLYGIKEDVFLSVPCVLGQNGIS
DVVKVTLTSEEEAHLKKSADTLWGIQKELQF
3D structure
PDB4i8x Fragment growing and linking lead to novel nanomolar lactate dehydrogenase inhibitors.
ChainH
Resolution2.23 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 6P3 H V30 T94 N137 R168 A237 T247 V30 T94 N137 R168 A237 T247 MOAD: Kd=2300uM
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:4i8x, PDBe:4i8x, PDBj:4i8x
PDBsum4i8x
PubMed23302067
UniProtP13491|LDHA_RABIT L-lactate dehydrogenase A chain (Gene Name=LDHA)

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