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TitleThe unusual active site of Gal6/bleomycin hydrolase can act as a carboxypeptidase, aminopeptidase, and peptide ligase.
Journal, issue, pagesCell(Cambridge,Mass. ), Vol. 93, Page 103-109, Year 1998
Publish dateFeb 27, 1998 (structure data deposition date)
AuthorsZheng, W. / Johnston, S.A. / Joshua-Tor, L.
External linksCell(Cambridge,Mass. ) / PubMed:9546396
MethodsX-ray diffraction
Resolution1.87 - 2.05 Å
Structure data

PDB-1a6r:
GAL6 (YEAST BLEOMYCIN HYDROLASE) MUTANT C73A
Method: X-RAY DIFFRACTION / Resolution: 2.05 Å

PDB-3gcb:
GAL6 (YEAST BLEOMYCIN HYDROLASE) MUTANT C73A/DELTAK454
Method: X-RAY DIFFRACTION / Resolution: 1.87 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

ChemComp-GOL:
GLYCEROL

Source
  • saccharomyces cerevisiae (brewer's yeast)
KeywordsHYDROLASE / BLEOMYCIN HYDROLASE / PEPTIDASE / PROTEASE / DNA-BINDING PROTEIN / SELF-COMPARTMENTALIZING PROTEASE

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