Structure of PDB 1dbv Chain P

Receptor sequence

>1dbvP (length=334) Species: 1422 (Geobacillus stearothermophilus)

AVKVGINGFGRIGRNVFRAALKNPDIEVVAVNGLTDANTLAHLLKYDSVH
GRLDAEVSVNGNNLVVNGKEIIVKAERDPENLAWGEIGVDIVVESTGRFT
KREDAAKHLEAGAKKVIISAPAKNEDITIVMGVNQDKYDPKAHHVISNAS
CTTNCLAPFAKVLHEQFGIVRGMMTTVHSYTNDQRILDASHKDLRRARAA
AESIIPTTTGAAKAVALVLPELKGKLNGMAMRVPTPNVSVVDLVAELEKE
VTVEEVNAALKAAAEGELKGILAYSEEPLVSRDYNGSTVSSTIDALSTMV
IDGKMVKVVSWYDNETGYSHRVVDLAAYIASKGL

3D structure

• PDB: 1dbv A crystallographic comparison between mutated glyceraldehyde-3-phosphate dehydrogenases from Bacillus stearothermophilus complexed with either NAD+ or NADP+.
• Chain: P
• Resolution: 2.5 Å

Enzymatic activity

• Enzyme Commision number: 1.2.1.12: glyceraldehyde-3-phosphate dehydrogenase (phosphorylating).

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	NAD	P	G7 G9 R10 I11 L33 S95 T96 G97 R98 F99 S119 C149 Y317	G8 G10 R11 I12 L34 S95 T96 G97 R98 F99 S119 C151 Y318

Gene Ontology

Molecular Function

• GO:0000166 nucleotide binding
• GO:0004365 glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
• GO:0016491 oxidoreductase activity
• GO:0016620 oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
• GO:0030554 adenyl nucleotide binding
• GO:0050661 NADP binding
• GO:0051287 NAD binding

Biological Process

• GO:0006006 glucose metabolic process
• GO:0006096 glycolytic process

Cellular Component

• GO:0005737 cytoplasm

External links

• PDB: RCSB:1dbv, PDBe:1dbv, PDBj:1dbv
• PDBsum: 1dbv
• PubMed: 9175858
• UniProt: P00362|G3P_GEOSE Glyceraldehyde-3-phosphate dehydrogenase (Gene Name=gap)