Structure of PDB 4i9u Chain F

Receptor sequence
>4i9uF (length=329) Species: 9986 (Oryctolagus cuniculus) [Search protein sequence]
AALKDQLIHNLLKEVPQNKITVVGVGAVGMACAISILMKDLADELALVDV
MEDKLKGEMMDLQHGSLFLRTPKIVSGKDYSVTANSKLVIITAGARQQEG
ESRLNLVQRNVNIFKFIIPNVVKYSPHCKLLVVSNPVDILTYVAWKISGF
PKNRVIGSGCNLDSARFRYLMGERLGVHALSCHGWILGEHGDSSVPVWSG
MNVAGVSLKTLHPELGTDADKEQWKQVHKQVVDSAYEVIKLKGYTTWAIG
LSVADLAESIMKNLRRVHPISTMLKGLYGIKEDVFLSVPCVLGQNGISDV
VKVTLTSEEEAHLKKSADTLWGIQKELQF
3D structure
PDB4i9u Fragment growing and linking lead to novel nanomolar lactate dehydrogenase inhibitors.
ChainF
Resolution2.5 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) R103 D163 R166 H190
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 1E7 F V25 G26 D51 V52 A95 R111 I115 F118 V23 G24 D49 V50 A93 R109 I113 F116 MOAD: Kd=137uM
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:4i9u, PDBe:4i9u, PDBj:4i9u
PDBsum4i9u
PubMed23302067
UniProtP13491|LDHA_RABIT L-lactate dehydrogenase A chain (Gene Name=LDHA)

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