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Structure paper

TitleCrystal structure and mechanism of human carboxypeptidase O: Insights into its specific activity for acidic residues.
Journal, issue, pagesProc. Natl. Acad. Sci. U.S.A., Vol. 115, Page E3932-E3939, Year 2018
Publish dateDec 27, 2016 (structure data deposition date)
AuthorsGarcia-Guerrero, M.C. / Garcia-Pardo, J. / Berenguer, E. / Fernandez-Alvarez, R. / Barfi, G.B. / Lyons, P.J. / Aviles, F.X. / Huber, R. / Lorenzo, J. / Reverter, D.
External linksProc. Natl. Acad. Sci. U.S.A. / PubMed:29636417
MethodsX-ray diffraction
Resolution1.854 Å
Structure data

PDB-5mrv:
Crystal structure of human carboxypeptidase O in complex with NvCI
Method: X-RAY DIFFRACTION / Resolution: 1.854 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
  • nerita versicolor (invertebrata)
KeywordsHYDROLASE / Digestive Metallocarboxypeptidase / food digestion / carboxypeptidase inhibitor / Brush Border enzyme

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