Structure of PDB 4i9n Chain H

Receptor sequence
>4i9nH (length=325) Species: 9986 (Oryctolagus cuniculus) [Search protein sequence]
AALKDQLIHNLLKEEHVPQNKITVVGVGAVGMACAISILMKDLADELALV
DVMEDKLKGEMMDLQHGSLFLRTPKIVSGKDYSVTANSKLVIITAGASRL
NLVQRNVNIFKFIIPNVVKYSPHCKLLVVSNPVDILTYVAWKISGFPKNR
VIGSGCNLDSARFRYLMGERLGVHALSCHGWILGEHGDSSVPVWSGMNVA
GVSLKTLHPELGTDADKEQWKQVHKQVVDSAYEVIKLKGYTTWAIGLSVA
DLAESIMKNLRRVHPISTMLKGLYGIKEDVFLSVPCVLGQNGISDVVKVT
LTSEEEAHLKKSADTLWGIQKELQF
3D structure
PDB4i9n Fragment growing and linking lead to novel nanomolar lactate dehydrogenase inhibitors.
ChainH
Resolution2.35 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) R99 D159 R162 H186
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 1E6 H G26 D51 V52 A95 G96 R111 I115 F118 I119 G26 D51 V52 A95 G96 R105 I109 F112 I113 MOAD: Kd=360uM
BS02 1E5 H G28 V30 T94 V135 S136 N137 R168 A237 T247 G28 V30 T94 V129 S130 N131 R162 A231 T241 MOAD: Kd=1300uM
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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Cellular Component
External links
PDB RCSB:4i9n, PDBe:4i9n, PDBj:4i9n
PDBsum4i9n
PubMed23302067
UniProtP13491|LDHA_RABIT L-lactate dehydrogenase A chain (Gene Name=LDHA)

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