Structure of PDB 4plh Chain B

Receptor sequence
>4plhB (length=313) Species: 5794 (Apicomplexa) [Search protein sequence]
QRKKISLIGAGNIGGTLAHLIAQKELGDVVLFDIVEGMPQGKALDISHSS
PIMGSNVKITGTNNYEDIKGSDVVIITAGIPRKPGMSRDDLLSVNAKIMK
DVAENIKKYCPNAFVIVVTNPLDVMVYVLHKYSGLPHNKVCGMAGVLDSS
RFRYFLAEKLNVSPNDVQAMVIGGHGDTMVPLTRYCTVGGIPLTEFIKQG
WITQEEIDEIVERTRNAGGEIVNLLKTGSAYFAPAASAIEMAESYLKDKK
RILPCSAYLEGQYGVKDLFVGVPVIIGKNGVEKIIELELTEEEQEMFDKS
VESVRELVETVKK
3D structure
PDB4plh An atomic-resolution view of neofunctionalization in the evolution of apicomplexan lactate dehydrogenases.
ChainB
Resolution1.9 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) R88 D148 R151 H175
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 B G13 N14 I15 D35 I36 T79 A80 G81 P83 I100 V120 N122 M145 H177 P236 G11 N12 I13 D33 I34 T77 A78 G79 P81 I98 V118 N120 M143 H175 P234
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
External links
PDB RCSB:4plh, PDBe:4plh, PDBj:4plh
PDBsum4plh
PubMed24966208
UniProtA0A075B5H2

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