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Structure paper

TitleThe structure of aspartyl dipeptidase reveals a unique fold with a Ser-His-Glu catalytic triad.
Journal, issue, pagesProc. Natl. Acad. Sci. USA, Vol. 97, Page 14097-14102, Year 2000
Publish dateSep 28, 2000 (structure data deposition date)
AuthorsHakansson, K. / Wang, A.H. / Miller, C.G.
External linksProc. Natl. Acad. Sci. USA / PubMed:11106384
MethodsX-ray diffraction
Resolution1.2 Å
Structure data

PDB-1fy2:
Aspartyl Dipeptidase
Method: X-RAY DIFFRACTION / Resolution: 1.2 Å

PDB-1fye:
Aspartyl Dipeptidase (Anisotropic B-Factor Refinement)
Method: X-RAY DIFFRACTION / Resolution: 1.2 Å

Chemicals

ChemComp-CD:
Unknown entry

ChemComp-HOH:
WATER

Source
  • salmonella typhimurium (bacteria)
KeywordsHYDROLASE / serine protease / peptidase / catalytic triad / strand-helix motif

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