Structure of PDB 1nqa Chain Q

Receptor sequence

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

AVKVGINGFGRIGRNVFRAALKNPDIEVVAVNDLTDANTLAHLLKYDSVH
GRLDAEVSVNGNNLVVNGKEIIVKAERDPENLAWGEIGVDIVVESTGRFT
KREDAAKHLEAGAKKVIISAPAKNEDITIVMGVNQDKYDPKAHHVISNAS
ATTNCLAPFAKVLHEQFGIVRGMMTTVHSYTNDQRILDLPHKDLRRARAA
AESIIPTTTGAAKAVALVLPELKGKLNGMAMRVPTPNVSVVDLVAELEKE
VTVEEVNAALKAAAEGELKGILAYSEEPLVSRDYNGSTVSSTIDALSTMV
IDGKMVKVVSWYDNETGYSHRVVDLAAYIASKGL

3D structure

• PDB: 1nqa Crystal structure of two ternary complexes of phosphorylating Glyceraldehyde-3-Phosphate Dehydrogenase from Bacillus stearothermophilus with NAD and D-Glyceraldehyde-3-Phosphate
• Chain: Q
• Resolution: 2.2 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	Q	G9 R10 I11 D32 L33 S95 T96 G97 R98 F99 S119 A149 N180 N313 Y317	G10 R11 I12 D33 L34 S95 T96 G97 R98 F99 S119 A151 N182 N314 Y318
BS02	G3H	Q	A149 T150 H176 T179 R231	A151 T152 H178 T181 R232

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:1nqa, PDBe:1nqa, PDBj:1nqa
• PDBsum: 1nqa
• PubMed: 12569100
• UniProt: P00362|G3P_GEOSE Glyceraldehyde-3-phosphate dehydrogenase (Gene Name=gap)