Structure of PDB 5fb3 Chain A

Receptor sequence

>5fb3A (length=336) Species: 410359 (Pyrobaculum calidifontis JCM 11548)

KVERFEVPRTIIFGPGALEKTPEVIPPSGRVLIITGKSSTRKYAERVAEL
LKQNCEIISYDQVELEKPGFDLVIGIGGGRPLDMAKVYSYIHKKPFVAIP
TSASHDGIASPYVSFSLTQRFSKYGKISSSPVAIIADTSIILSAPSRLLK
AGIGDLLGKIIAVRDWQLAHRLKGEEYSEYAAHLSLTSYKIAVGNAQKIK
NFIREEDVRVLVKALIGCGVAMGIAGSSRPCSGSEHLFAHAIEVRVEKED
EVVHGELVALGTIIMAYLHGINWRRIKRIADIIGLPTSLRQANIDVDLAL
EALTTAHTLRPDRYTILGDGLSREAAKRALEDVELI

3D structure

• PDB: 5fb3 Unique coenzyme binding mode of hyperthermophilic archaeal sn-glycerol-1-phosphate dehydrogenase from Pyrobaculum calidifontis
• Chain: A
• Resolution: 2.45 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): D157 H238 A241 H256
• Catalytic site (residue number reindexed from 1): D155 H236 A239 H254
• Enzyme Commision number: 1.1.1.261: sn-glycerol-1-phosphate 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	ZN	A	D157 H238 H256	D155 H236 H254

Gene Ontology

Molecular Function

• GO:0016491 oxidoreductase activity
• GO:0016614 oxidoreductase activity, acting on CH-OH group of donors
• GO:0046872 metal ion binding
• GO:0050492 glycerol-1-phosphate dehydrogenase [NAD(P)+] activity
• GO:0106357 glycerol-1-phosphate dehydrogenase (NAD+) activity
• GO:0106358 glycerol-1-phosphate dehydrogenase (NADP+) activity

Biological Process

• GO:0006650 glycerophospholipid metabolic process
• GO:0008654 phospholipid biosynthetic process

Cellular Component

• GO:0005737 cytoplasm

External links

• PDB: RCSB:5fb3, PDBe:5fb3, PDBj:5fb3
• PDBsum: 5fb3
• PubMed: 27616573
• UniProt: A3MTM6|G1PDH_PYRCJ Glycerol-1-phosphate dehydrogenase [NAD(P)+] (Gene Name=egsA)