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Structure paper

TitleOn the role of the conformational flexibility of the active-site lid on the allosteric kinetics of glucosamine-6-phosphate deaminase.
Journal, issue, pagesJ. Mol. Biol., Vol. 319, Page 183-189, Year 2002
Publish dateAug 20, 2001 (structure data deposition date)
AuthorsBustos-Jaimes, I. / Sosa-Peinado, A. / Rudino-Pinera, E. / Horjales, E. / Calcagno, M.L.
External linksJ. Mol. Biol. / PubMed:12051945
MethodsX-ray diffraction
Resolution2.06 Å
Structure data

PDB-1jt9:
Structure of the mutant F174A T form of the Glucosamine-6-Phosphate deaminase from E.coli
Method: X-RAY DIFFRACTION / Resolution: 2.06 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • escherichia coli (E. coli)
KeywordsHYDROLASE / ALLOSTERIC ENZYME / ENTROPIC EFFECTS / ALDOSE-KETOSE ISOMERASE / STRUCTURAL FLEXIBILITY

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