Structure of PDB 4i9u Chain E

Receptor sequence

>4i9uE (length=331) Species: 9986 (Oryctolagus cuniculus)

AALKDQLIHNLLKEEHVPQNKITVVGVGAVGMACAISILMKDLADELALV
DVMEDKLKGEMMDLQHGSLFLRTPKIVSGKDYSVTANSKLVIITAGARQQ
EGESRLNLVQRNVNIFKFIIPNVVKYSPHCKLLVVSNPVDILTYVAWKIS
GFPKNRVIGSGCNLDSARFRYLMGERLGVHALSCHGWILGEHGDSSVPVW
SGMNVAGVSLKTLHPELGTDADKEQWKQVHKQVVDSAYEVIKLKGYTTWA
IGLSVADLAESIMKNLRRVHPISTMLKGLYGIKEDVFLSVPCVLGQNGIS
DVVKVTLTSEEEAHLKKSADTLWGIQKELQF

3D structure

• PDB: 4i9u Fragment growing and linking lead to novel nanomolar lactate dehydrogenase inhibitors.
• Chain: E
• Resolution: 2.5 Å

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	1E7	E	G26 D51 V52 A95 R98 R111 I115 F118 I119	G26 D51 V52 A95 R98 R111 I115 F118 I119	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

External links

• PDB: RCSB:4i9u, PDBe:4i9u, PDBj:4i9u
• PDBsum: 4i9u
• PubMed: 23302067
• UniProt: P13491|LDHA_RABIT L-lactate dehydrogenase A chain (Gene Name=LDHA)