BioLiP

Structure of PDB 4plh Chain D

Receptor sequence

>4plhD (length=316) Species: 5794 (Apicomplexa) [Search protein sequence]

TQRKKISLIGAGNIGGTLAHLIAQKELGDVVLFDIVEGMPQGKALDISHS
SPIMGSNVKITGTNNYEDIKGSDVVIITAGIPRKPGMSRDDLLSVNAKIM
KDVAENIKKYCPNAFVIVVTNPLDVMVYVLHKYSGLPHNKVCGMAGVLDS
SRFRYFLAEKLNVSPNDVQAMVIGGHGDTMVPLTRYCTVGGIPLTEFIKQ
GWITQEEIDEIVERTRNAGGEIVNLLKTGSAYFAPAASAIEMAESYLKDK
KRILPCSAYLEGQYGVKDLFVGVPVIIGKNGVEKIIELELTEEEQEMFDK
SVESVRELVETVKKLN

3D structure

PDB

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

Chain

Resolution

1.9 Å

3D
structure

Catalytic site residues are labeled in the structure
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Enzymatic activity

Catalytic site (original residue number in PDB)	R90 D150 R153 H177
Catalytic site (residue number reindexed from 1)	R89 D149 R152 H176
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	G13 N14 I15 D35 I36 T79 A80 G81 I100 V120 N122 M145 L149 H177 P236	G12 N13 I14 D34 I35 T78 A79 G80 I99 V119 N121 M144 L148 H176 P235

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:4plh, PDBe:4plh, PDBj:4plh
PDBsum	4plh
PubMed	24966208
UniProt	A0A075B5H2