Structure of PDB 3vph Chain C

Receptor sequence
>3vphC (length=310) Species: 272 (Thermus caldophilus) [Search protein sequence]
MKVGIVGSGMVGSATAYALALLGVAREVVLVDLDRKLAQAHAEDILHATP
FAHPVWVRAGSYGDLEGARAVVLAAGVAQRPGETRLQLLDRNAQVFAQVV
PRVLEAAPEAVLLVATNPVDVMTQVAYRLSALPPGRVVGSGTILDTARFR
ALLAEHLRVAPQSVHAYVLGEHGDSEVLVWSSAQVGGVPLLEFAEARGRA
LSPEDRARIDEGVRRAAYRIIEGKGATYYGIGAGLARLVRAILTDEKGVY
TVSAFTPEVEGVLEVSLSLPRILGAGGVEGTVYPSLSPEEREALRRSAEI
LKEAAFALGF
3D structure
PDB3vph The core of allosteric motion in Thermus caldophilus L-lactate dehydrogenase.
ChainC
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R106 D166 R169 H193
Catalytic site (residue number reindexed from 1) R85 D145 R148 H172
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 FBP C R171 Q183 H186 Y188 R150 Q162 H165 Y167
Gene Ontology
Molecular Function
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:0006096 glycolytic process
GO:0019752 carboxylic acid metabolic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3vph, PDBe:3vph, PDBj:3vph
PDBsum3vph
PubMed25258319
UniProtP06150|LDH_THECA L-lactate dehydrogenase (Gene Name=ldh)

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