Structure of PDB 5nqq Chain C

Receptor sequence

>5nqqC (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: C
• 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	C	G28 A29 V30 D51 V52 M53 K56 T94 A95 G96 A97 R98 V135 N137 H192 I251	G28 A29 V30 D51 V52 M53 K56 T94 A95 G96 A97 R98 V135 N137 H192 I251
BS02	OAA	C	Q99 R105 N137 R168 H192 A237 T247	Q99 R105 N137 R168 H192 A237 T247	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)