Structure of PDB 3vph Chain A

Receptor sequence

>3vphA (length=310) Species: 272 (Thermus caldophilus)

MKVGIVGSGMVGSATAYALALLGVAREVVLVDLDRKLAQAHAEDILHATP
FAHPVWVRAGSYGDLEGARAVVLAAGVAQRPGETRLQLLDRNAQVFAQVV
PRVLEAAPEAVLLVATNPVDVMTQVAYRLSALPPGRVVGSGTILDTARFR
ALLAEHLRVAPQSVHAYVLGEHGDSEVLVWSSAQVGGVPLLEFAEARGRA
LSPEDRARIDEGVRRAAYRIIEGKGATYYGIGAGLARLVRAILTDEKGVY
TVSAFTPEVEGVLEVSLSLPRILGAGGVEGTVYPSLSPEEREALRRSAEI
LKEAAFALGF

3D structure

• PDB: 3vph The core of allosteric motion in Thermus caldophilus L-lactate dehydrogenase.
• Chain: A
• Resolution: 2.0 Å

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	A	R171 Q183 H186 Y188	R150 Q162 H165 Y167
BS02	NAD	A	G29 M30 V31 D52 L53 Y83 A96 G97 V120 A136 N138 H193 T247 I251	G9 M10 V11 D32 L33 Y62 A75 G76 V99 A115 N117 H172 T227 I231

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

External links

• PDB: RCSB:3vph, PDBe:3vph, PDBj:3vph
• PDBsum: 3vph
• PubMed: 25258319
• UniProt: P06150|LDH_THECA L-lactate dehydrogenase (Gene Name=ldh)