Structure of PDB 1hdg Chain O

Receptor sequence
>1hdgO (length=332) Species: 2336 (Thermotoga maritima) [Search protein sequence]
ARVAINGFGRIGRLVYRIIYERKNPDIEVVAINDLTDTKTLAHLLKYDSV
HKKFPGKVEYTENSLIVDGKEIKVFAEPDPSKLPWKDLGVDFVIESTGVF
RNREKAELHLQAGAKKVIITAPAKGEDITVVIGCNEDQLKPEHTIISCAS
CTTNSIAPIVKVLHEKFGIVSGMLTTVHSYTNDQRVLDLPHKDLRRARAA
AVNIIPTTTGAAKAVALVVPEVKGKLDGMAIRVPTPDGSITDLTVLVEKE
TTVEEVNAVMKEATEGRLKGIIGYNDEPIVSSDIIGTTFSGIFDATITNV
IGGKLVKVASWYDNEYGYSNRVVDTLELLLKM
3D structure
PDB1hdg The crystal structure of holo-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima at 2.5 A resolution.
ChainO
Resolution2.5 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 NAD O G9 R10 I11 D32 L33 P77 T96 G97 T119 N180 N313 Y317 G9 R10 I11 D34 L35 P78 T97 G98 T120 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: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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Cellular Component
External links
PDB RCSB:1hdg, PDBe:1hdg, PDBj:1hdg
PDBsum1hdg
PubMed7877172
UniProtP17721|G3P_THEMA Glyceraldehyde-3-phosphate dehydrogenase (Gene Name=gap)

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