Structure of PDB 4ply Chain B

Receptor sequence
>4plyB (length=318) Species: 5794 (Apicomplexa) [Search protein sequence]
QRKKISLIGAGNIGGTLAHLIAQKELGDVVLFDIVEGMPQGKALDISHSS
PIMGSNVKITGTNNYEDIKGSDVVIITAGIPRKPGKSDKEWSRDDLLSVN
AKIMKDVAENIKKYCPNAFVIVVTNPLDVMVYVLHKYSGLPHNKVCGMAG
VLDSSRFRYFLAEKLNVSPNDVQAMVIGGHGDTMVPLTRYCTVGGIPLTE
FIKQGWITQEEIDEIVERTRNAGGEIVNLLKTGSAYFAPAASAIEMAESY
LKDKKRILPCSAYLEGQYGVKDLFVGVPVIIGKNGVEKIIELELTEEEQE
MFDKSVESVRELVETVKK
3D structure
PDB4ply 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) 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 B G13 N14 I15 D35 I36 T79 A80 G81 I82 P83 I105 V125 N127 M150 H182 P241 G11 N12 I13 D33 I34 T77 A78 G79 I80 P81 I103 V123 N125 M148 H180 P239
BS02 PYR B W93 R95 R158 H182 G225 W91 R93 R156 H180 G223
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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