Structure of PDB 4ply Chain H

Receptor sequence
>4plyH (length=303) Species: 5794 (Apicomplexa) [Search protein sequence]
QRKKISLIGAGNIGGTLAHLIAQKELGDVVLFDIVEGMPQGKALDISHSS
PIMGSNVKITGTNNYEDIKGSDVVIITAGDLLSVNAKIMKDVAENIKKYC
PNAFVIVVTNPLDVMVYVLHKYSGLPHNKVCGMAGVLDSSRFRYFLAEKL
NVSPNDVQAMVIGGHGDTMVPLTRYCTVGGIPLTEFIKQGWITQEEIDEI
VERTRNAGGEIVNLLKTGSAYFAPAASAIEMAESYLKDKKRILPCSAYLE
GQYGVKDLFVGVPVIIGKNGVEKIIELELTEEEQEMFDKSVESVRELVET
VKK
3D structure
PDB4ply An atomic-resolution view of neofunctionalization in the evolution of apicomplexan lactate dehydrogenases.
ChainH
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) D155 R158 H182
Catalytic site (residue number reindexed from 1) D138 R141 H165
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 H G13 N14 I15 D35 I36 T79 A80 I105 V125 N127 M150 H182 P241 G11 N12 I13 D33 I34 T77 A78 I88 V108 N110 M133 H165 P224
BS02 PYR H N127 R158 H182 G225 N110 R141 H165 G208
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:4ply, PDBe:4ply, PDBj:4ply
PDBsum4ply
PubMed24966208
UniProtA0A075B5H0

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