Structure of PDB 1nq5 Chain A

Receptor sequence

>1nq5A (length=334) Species: 1422 (Geobacillus stearothermophilus)

AVKVGINGFGRIGRNVFRAALKNPDIEVVAVNDLTDANTLAHLLKYDSVH
GRLDAEVSVNGNNLVVNGKEIIVKAERDPENLAWGEIGVDIVVESTGRFT
KREDAAKHLEAGAKKVIISAPAKNEDITIVMGVNQDKYDPKAHHVISNAS
STTNCLAPFAKVLHEQFGIVRGMMTTVHSYTNDQRILDLPHKDLRRARAA
AESIIPTTTGAAKAVALVLPELKGKLNGMAMRVPTPNVSVVDLVAELEKE
VTVEEVNAALKAAAEGELKGILAYSEEPLVSRDYNGSTVSSTIDALSTMV
IDGKMVKVVSWYDNETGYSHRVVDLAAYIASKGL

3D structure

• PDB: 1nq5 Crystal structure of two ternary complexes of phosphorylating Glyceraldehyde-3-Phosphate Dehydrogenase from Bacillus stearothermophilus with NAD and D-Glyceraldehyde-3-Phosphate
• Chain: A
• Resolution: 2.11 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): S149 H176
• Catalytic site (residue number reindexed from 1): S151 H178
• 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	A	G9 R10 I11 D32 L33 S95 T96 G97 S119 T179 N180 N313 Y317	G10 R11 I12 D33 L34 S95 T96 G97 S119 T181 N182 N314 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:1nq5, PDBe:1nq5, PDBj:1nq5
• PDBsum: 1nq5
• PubMed: 12569100
• UniProt: P00362|G3P_GEOSE Glyceraldehyde-3-phosphate dehydrogenase (Gene Name=gap)