Structure of PDB 2dbv Chain O

Receptor sequence
>2dbvO (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+.
ChainO
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 O G7 G9 R10 I11 N31 G32 L33 R77 S95 T96 G97 S119 C149 N313 Y317 G8 G10 R11 I12 N32 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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