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TitleSubstrate specificity and reaction mechanism of human prolidase.
Journal, issue, pagesFEBS J., Vol. 284, Page 2870-2885, Year 2017
Publish dateOct 18, 2016 (structure data deposition date)
AuthorsWilk, P. / Uehlein, M. / Kalms, J. / Dobbek, H. / Mueller, U. / Weiss, M.S.
External linksFEBS J. / PubMed:28677335
MethodsX-ray diffraction
Resolution1.48 - 1.73 Å
Structure data

PDB-5m4g:
Crystal Structure of Wild-Type Human Prolidase with Mn ions
Method: X-RAY DIFFRACTION / Resolution: 1.48 Å

PDB-5m4j:
Crystal Structure of Wild-Type Human Prolidase with GlyPro ligand
Method: X-RAY DIFFRACTION / Resolution: 1.55 Å

PDB-5m4l:
Crystal Structure of Wild-Type Human Prolidase with Mg ions and LeuPro ligand
Method: X-RAY DIFFRACTION / Resolution: 1.49 Å

PDB-5m4q:
Crystal Structure of Wild-Type Human Prolidase with Mn ions and Pro ligand
Method: X-RAY DIFFRACTION / Resolution: 1.73 Å

Chemicals

ChemComp-MN:
Unknown entry

ChemComp-OH:
HYDROXIDE ION

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

ChemComp-NA:
Unknown entry

ChemComp-GLY:
GLYCINE

ChemComp-PRO:
PROLINE

ChemComp-MG:
Unknown entry

ChemComp-LEU:
LEUCINE

Source
  • homo sapiens (human)
KeywordsHYDROLASE / prolidase / peptidase / hydrolysis / pita-bread / metalloenzyme / hydroxide ion

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