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Structure paper

TitleNovel inhibitor for prolyl tripeptidyl aminopeptidase from Porphyromonas gingivalis and details of substrate-recognition mechanism
Journal, issue, pagesJ. Mol. Biol., Vol. 375, Page 708-719, Year 2008
Publish dateFeb 16, 2007 (structure data deposition date)
AuthorsXu, Y. / Nakajima, Y. / Ito, K. / Zheng, H. / Oyama, H. / Heiser, U. / Hoffmann, T. / Gartner, U.T. / Demuth, H.U. / Yoshimoto, T.
External linksJ. Mol. Biol. / PubMed:18042490
MethodsX-ray diffraction
Resolution1.95 - 2.2 Å
Structure data

PDB-2eep:
Prolyl Tripeptidyl Aminopeptidase Complexed with an Inhibitor
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

PDB-2z3w:
Prolyl tripeptidyl aminopeptidase mutant E636A
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-2z3z:
Prolyl tripeptidyl aminopeptidase mutant E636A complexd with an inhibitor
Method: X-RAY DIFFRACTION / Resolution: 1.95 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-AIO:
[(2R)-1-(L-ALANYL-L-ISOLEUCYL)PYRROLIDIN-2-YL]BORONIC ACID

ChemComp-HOH:
WATER

ChemComp-GOL:
GLYCEROL

Source
  • porphyromonas gingivalis (bacteria)
KeywordsHYDROLASE / peptidase family S9 / prolyl oligopeptidase family / serine peptidase / inhibitor complex / serine protease / proline-specific peptidase

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