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Structure paper

TitleHydrogen bonding and catalysis: a novel explanation for how a single amino acid substitution can change the pH optimum of a glycosidase.
Journal, issue, pagesJ. Mol. Biol., Vol. 299, Page 255-279, Year 2000
Publish dateNov 24, 1999 (structure data deposition date)
AuthorsJoshi, M.D. / Sidhu, G. / Pot, I. / Brayer, G.D. / Withers, S.G. / McIntosh, L.P.
External linksJ. Mol. Biol. / PubMed:10860737
MethodsX-ray diffraction
Resolution1.55 - 1.8 Å
Structure data

PDB-1c5h:
HYDROGEN BONDING AND CATALYSIS: AN UNEXPECTED EXPLANATION FOR HOW A SINGLE AMINO ACID SUBSTITUTION CAN CHANGE THE PH OPTIMUM OF A GLYCOSIDASE
Method: X-RAY DIFFRACTION / Resolution: 1.55 Å

PDB-1c5i:
HYDROGEN BONDING AND CATALYSIS: AN UNEXPECTED EXPLANATION FOR HOW A SINGLE AMINO ACID SUBSTITUTION CAN CHANGE THE PH OPTIMUM OF A GLYCOSIDASE
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • bacillus circulans (bacteria)
KeywordsHYDROLASE / GLYCOSIDASE / PH-DEPENDENT ENZYME MECHANISM / GENERAL ACID/ BASE CATALYSIS / X-RAY CYRSTALLOGRAPHY / ISOTOPE SHIFT / SHORT HYDROGEN BONDS / XYLAN

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