Structure of PDB 2g82 Chain R

Receptor sequence
>2g82R (length=330) Species: 271 (Thermus aquaticus) [Search protein sequence]
MKVGINGFGRIGRQVFRILHSRGVEVALINDLTDNKTLAHLLKYDSIYHR
FPGEVAYDDQYLYVDGKAIRATAVKDPKEIPWAEAGVGVVIESTGVFTDA
DKAKAHLEGGAKKVIITAPAKGEDITIVMGVNHEAYDPSRHHIISNASCT
TNSLAPVMKVLEEAFGVEKALMTTVHSYTNDQRLLDLPHKDLRRARAAAI
NIIPTTTGAAKATALVLPSLKGRFDGMALRVPTATGSISDITALLKREVT
AEEVNAALKAAAEGPLKGILAYTEDEIVLQDIVMDPHSSIVDAKLTKALG
NMVKVFAWYDNEWGYANRVADLVELVLRKG
3D structure
PDB2g82 High Resolution Structures of Thermus aquaticus Glyceraldehyde-3-Phosphate Dehydrogenase: Role of 220's Loop Motion in Catalysis
ChainR
Resolution1.65 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 R G9 R10 I11 D31 L32 T94 G95 F97 T117 A149 N180 N311 Y315 G9 R10 I11 D31 L32 T94 G95 F97 T117 A149 N180 N311 Y315
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:2g82, PDBe:2g82, PDBj:2g82
PDBsum2g82
PubMed
UniProtP00361|G3P_THEAQ Glyceraldehyde-3-phosphate dehydrogenase (Gene Name=gap)

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