BioLiP

Structure of PDB 4plv Chain C

Receptor sequence

>4plvC (length=318) Species: 5794 (Apicomplexa) [Search protein sequence]

QRKKISLIGAGNIGGTLAHLIAQKELGDVVLFDIVEGMPQGKALDISHSS
PIMGSNVKITGTNNYEDIKGSDVVIITAGIPRKPGKSDKEWSRDDLLSVN
AKIMKDVAENIKKYCPNAFVIVVTNPLDVMVYVLHKYSGLPHNKVCGMAG
VLDSSRFRYFLAEKLNVSPNDVQAMVIGGHGDTMVPLTRYCTVGGIPLTE
FIKQGWITQEEIDEIVERTRNAGGEIVNLLKTGSAYFAPAASAIEMAESY
LKDKKRILPCSAYLEGQYGVKDLFVGVPVIIGKNGVEKIIELELTEEEQE
MFDKSVESVRELVETVKK

3D structure

PDB

4plv An atomic-resolution view of neofunctionalization in the evolution of apicomplexan lactate dehydrogenases.

Chain

Resolution

1.85 Å

3D
structure

Catalytic site residues are labeled in the structure
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Enzymatic activity

Catalytic site (original residue number in PDB)	D155 R158 H182
Catalytic site (residue number reindexed from 1)	D153 R156 H180
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	G13 N14 I15 D35 I36 T79 A80 G81 P83 I105 V125 N127 M150 H182 P241	G11 N12 I13 D33 I34 T77 A78 G79 P81 I103 V123 N125 M148 H180 P239

Gene Ontology

	Molecular Function
GO:0000166	nucleotide binding
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

View graph for
Molecular Function

View graph for
Biological Process

PDB	RCSB:4plv, PDBe:4plv, PDBj:4plv
PDBsum	4plv
PubMed	24966208
UniProt	A0A075B5H0