Structure of PDB 4plc Chain C

Receptor sequence
>4plcC (length=324) Species: 5794 (Apicomplexa) [Search protein sequence]
MTKRKKISLIGSGMIGGTMAYLCAQKELGDVVLFDVVKNMPQGKALDLSH
SSSIADTNVKVTGTNSYEDIKGSDVVIITAGLTKAPGKSDKEWSRDDLLP
FNAKIMREVGENIKKYCPNAFVIVITNPLDVMVKVLHEHSGLPKNKVCGM
AGVLDSSRFRHFIAEKLNVSPRDVQAMVIGAHGDKMVPLTRYVTVNGIPL
QEFIKKGRITQEEIDEIVERTKNAGGEIVNLLGQGSAYFAPAASAIEMAE
AYLKDKKRVLVCSCYLEGQYGHKDMFVGVPAVIGGNGVEKVIELELTPEE
KELFDKSVEEVRKLQKAIKALGLE
3D structure
PDB4plc An atomic-resolution view of neofunctionalization in the evolution of apicomplexan lactate dehydrogenases.
ChainC
Resolution1.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R99 D159 R162 H186
Catalytic site (residue number reindexed from 1) R95 D155 R158 H182
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 PYR C W97 R99 N131 R162 H186 G229 W93 R95 N127 R158 H182 G225
BS02 NAI C G17 M18 I19 D39 V40 T83 A84 L86 T87 I109 E112 I129 T130 N131 M154 H186 P245 G13 M14 I15 D35 V36 T79 A80 L82 T83 I105 E108 I125 T126 N127 M150 H182 P241
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:4plc, PDBe:4plc, PDBj:4plc
PDBsum4plc
PubMed24966208
UniProtA0A075B5G8

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