Structure of PDB 5nqq Chain D

Receptor sequence

>5nqqD (length=331) Species: 9986 (Oryctolagus cuniculus)

AALKDQLIHNLLKEEHVPQNKITVVGVGAVGMACAISILMKDLADELALV
DVMEDKLKGEMMDLQHGSLFLRTPKIVSGKDYSVTANSKLVIITAGARQQ
EGESRLNLVQRNVNIFKFIIPNVVKYSPHCKLLVVSNPVDILTYVAWKIS
GFPKNRVIGSGCNLDSARFRYLMGERLGVHALSCHGWILGEHGDSSVPVW
SGMNVAGVSLKTLHPELGTDADKEQWKQVHKQVVDSAYEVIKLKGYTSWA
IGLSVADLAESIMKNLRRVHPISTMLKGLYGIKEDVFLSVPCVLGQNGIS
DVVKVTLTSEEEAHLKKSADTLWGIQKELQF

3D structure

• PDB: 5nqq The self-inhibitory nature of metabolic networks and its alleviation through compartmentalization.
• Chain: D
• Resolution: 1.872 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	NAI	D	G28 A29 V30 D51 V52 M53 K56 T94 A95 G96 V135 N137 I251	G28 A29 V30 D51 V52 M53 K56 T94 A95 G96 V135 N137 I251
BS02	OAA	D	N137 R168 H192 A237	N137 R168 H192 A237	MOAD: Ki=2.3mM

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:5nqq, PDBe:5nqq, PDBj:5nqq
• PDBsum: 5nqq
• PubMed: 28691704
• UniProt: P13491|LDHA_RABIT L-lactate dehydrogenase A chain (Gene Name=LDHA)