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Structure paper

TitleInsight into the substrate length restriction of M32 carboxypeptidases: Characterization of two distinct subfamilies.
Journal, issue, pagesProteins, Vol. 77, Page 647-657, Year 2009
Publish dateJun 1, 2009 (structure data deposition date)
AuthorsLee, M.M. / Isaza, C.E. / White, J.D. / Chen, R.P. / Liang, G.F. / He, H.T. / Chan, S.I. / Chan, M.K.
External linksProteins / PubMed:19544567
MethodsX-ray diffraction
Resolution2.1 - 2.9 Å
Structure data

PDB-3hoa:
Crystal structure of the Thermus thermophilus M32 carboxypeptidase
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-3hq2:
BsuCP Crystal Structure
Method: X-RAY DIFFRACTION / Resolution: 2.9 Å

Chemicals

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

ChemComp-ZN:
Unknown entry

ChemComp-PO4:
PHOSPHATE ION

ChemComp-CL:
Unknown entry

ChemComp-F:
FLUORIDE ION

Source
  • thermus thermophilus hb27 (bacteria)
  • bacillus subtilis (bacteria)
KeywordsHYDROLASE / proline-rich loop / Carboxypeptidase / Metal-binding / Metalloprotease / Protease / Zinc

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