Structure of PDB 4i9h Chain B

Receptor sequence
>4i9hB (length=327) Species: 9986 (Oryctolagus cuniculus) [Search protein sequence]
AALKDQLIHNLLKEEHVPQNKITVVGVGAVGMACAISILMKDLADELALV
DVMEDKLKGEMMDLQHGSLFLRTPKIVSGKDYSVTANSKLVIITAGARQS
RLNLVQRNVNIFKFIIPNVVKYSPHCKLLVVSNPVDILTYVAWKISGFPK
NRVIGSGCNLDSARFRYLMGERLGVHALSCHGWILGEHGDSSVPVWSGMN
VAGVSLKTLHPELGTDADKEQWKQVHKQVVDSAYEVIKLKGYTTWAIGLS
VADLAESIMKNLRRVHPISTMLKGLYGIKEDVFLSVPCVLGQNGISDVVK
VTLTSEEEAHLKKSADTLWGIQKELQF
3D structure
PDB4i9h Fragment growing and linking lead to novel nanomolar lactate dehydrogenase inhibitors.
ChainB
Resolution2.17 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) L105 D165 R168 H192
Catalytic site (residue number reindexed from 1) L102 D161 R164 H188
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 1E4 B G26 V30 D51 V52 T94 A95 G96 R111 I115 F118 I119 V135 S136 N137 R168 A237 T247 G26 V30 D51 V52 T94 A95 G96 R107 I111 F114 I115 V131 S132 N133 R164 A233 T243 MOAD: Kd=0.068uM
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:4i9h, PDBe:4i9h, PDBj:4i9h
PDBsum4i9h
PubMed23302067
UniProtP13491|LDHA_RABIT L-lactate dehydrogenase A chain (Gene Name=LDHA)

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