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EBI PDBe PDBeView

PDBe Entry: 1gae view

COMPARISON OF THE STRUCTURES OF WILD TYPE AND A N313T MUTANT OF ESCHERICHIA COLI GLYCERALDEHYDE 3-PHOSPHATE DEHYDROGENASES: IMPLICATION FOR NAD BINDING AND COOPERATIVITY
Summary
Header OXIDOREDUCTASE (ALDEHYDE(D)-NAD+(A))search
Method X-RAY DIFFRACTION
Experiment Resolution: 2.17 Å, R-factor: 20.6%, Spacegroup: C 2 2 21
Released 08/03/1996, deposition: 24/10/1995, last revision: 24/02/2009
Authors Duee, E.search; Olivier-Deyris, L.search; Fanchon, E.search; Corbier, C.search; Branlant, G.search; Dideberg, O.search
Primary citation Comparison of the structures of wild-type and a N313T mutant of Escherichia coli glyceraldehyde 3-phosphate dehydrogenases: implication for NAD binding and cooperativity.
J.MOL.BIOL.search vol:257, pag:814-838 (1996) [PubMed ID 8636984 ]search
Keywords OXIDOREDUCTASE (ALDEHYDE(D)-NAD+(A))search
EC 1.2.1.12 ExPASy BRENDA search (O P)
Organism Escherichia coli 562search(O P)
UniProt Glyceraldehyde-3-phosphate dehydrogenase A (EC 1.2.1.12) (GAPDH-A) P0A9B2search (O P)
Solvent O, P
Polymers
Id Name Type UniProt Residues Observed
O, P D-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE Protein P0A9B2 (G3P1_ECOLI)search
 330 100%
Heterogens
Id Name Ligands
O, P NICOTINAMIDE-ADENINE-DINUCLEOTIDE NAD search
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