Structure of PDB 2dbv Chain Q

Receptor sequence
>2dbvQ (length=334) Species: 1422 (Geobacillus stearothermophilus) [Search protein sequence]
AVKVGINGFGRIGRNVFRAALKNPDIEVVAVNGLTDANTLAHLLKYDSVH
GRLDAEVSVNGNNLVVNGKEIIVKAERDPENLAWGEIGVDIVVESTGRFT
KREDAAKHLEAGAKKVIISAPAKNEDITIVMGVNQDKYDPKAHHVISNAS
CTTNCLAPFAKVLHEQFGIVRGMMTTVHSYTNDQRILDASHKDLRRARAA
AESIIPTTTGAAKAVALVLPELKGKLNGMAMRVPTPNVSVVDLVAELEKE
VTVEEVNAALKAAAEGELKGILAYSEEPLVSRDYNGSTVSSTIDALSTMV
IDGKMVKVVSWYDNETGYSHRVVDLAAYIASKGL
3D structure
PDB2dbv A crystallographic comparison between mutated glyceraldehyde-3-phosphate dehydrogenases from Bacillus stearothermophilus complexed with either NAD+ or NADP+.
ChainQ
Resolution2.2 Å
3D
structure
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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 NDP Q G9 R10 I11 G32 L33 R77 S95 T96 G97 S119 C149 N313 Y317 G10 R11 I12 G33 L34 R77 S95 T96 G97 S119 C151 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

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:2dbv, PDBe:2dbv, PDBj:2dbv
PDBsum2dbv
PubMed9175858
UniProtP00362|G3P_GEOSE Glyceraldehyde-3-phosphate dehydrogenase (Gene Name=gap)

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