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Structure paper

TitleComparison of the structures of wild-type and a N313T mutant of Escherichia coli glyceraldehyde 3-phosphate dehydrogenases: implication for NAD binding and cooperativity.
Journal, issue, pagesJ. Mol. Biol., Vol. 257, Page 814-838, Year 1996
Publish dateOct 24, 1995 (structure data deposition date)
AuthorsDuee, E. / Olivier-Deyris, L. / Fanchon, E. / Corbier, C. / Branlant, G. / Dideberg, O.
External linksJ. Mol. Biol. / PubMed:8636984
MethodsX-ray diffraction
Resolution1.8 - 2.17 Å
Structure data

PDB-1gad:
COMPARISON OF THE STRUCTURES OF WILD TYPE AND A N313T MUTANT OF ESCHERICHIA COLI GLYCERALDEHYDE 3-PHOSPHATE DEHYDROGENASES: IMPLICATION FOR NAD BINDING AND COOPERATIVITY
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-1gae:
COMPARISON OF THE STRUCTURES OF WILD TYPE AND A N313T MUTANT OF ESCHERICHIA COLI GLYCERALDEHYDE 3-PHOSPHATE DEHYDROGENASES: IMPLICATION FOR NAD BINDING AND COOPERATIVITY
Method: X-RAY DIFFRACTION / Resolution: 2.17 Å

Chemicals

ChemComp-NAD:
NICOTINAMIDE-ADENINE-DINUCLEOTIDE / NAD*YM

ChemComp-HOH:
WATER

Source
  • escherichia coli (E. coli)
KeywordsOXIDOREDUCTASE (ALDEHYDE(D)-NAD+(A))

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