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TitleMutational and structural analysis of L-N-carbamoylase reveals new insights into a peptidase m20/m25/m40 family member.
Journal, issue, pagesJ. Bacteriol., Vol. 194, Page 5759-5768, Year 2012
Publish dateMay 25, 2010 (structure data deposition date)
AuthorsMartinez-Rodriguez, S. / Garcia-Pino, A. / Las Heras-Vazquez, F.J. / Clemente-Jimenez, J.M. / Rodriguez-Vico, F. / Garcia-Ruiz, J.M. / Loris, R. / Gavira, J.A.
External linksJ. Bacteriol. / PubMed:22904279
MethodsX-ray diffraction
Resolution2.75 Å
Structure data

PDB-3n5f:
Crystal Structure of L-N-carbamoylase from Geobacillus stearothermophilus CECT43
Method: X-RAY DIFFRACTION / Resolution: 2.75 Å

Chemicals

ChemComp-IPA:
ISOPROPYL ALCOHOL / alkaloid*YM

ChemComp-CO:
Unknown entry

ChemComp-CAC:
CACODYLATE ION

ChemComp-HOH:
WATER

Source
  • bacillus stearothermophilus (bacteria)
KeywordsHYDROLASE / Carbamoylase / hinge domain / M20 peptidase family / evolution / binding residue / dimerization domain

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