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Structure paper

TitleAtomic Resolution Analysis of the Catalytic Site of an Aspartic Proteinase and an Unexpected Mode of Binding by Short Peptides
Journal, issue, pagesProtein Sci., Vol. 12, Page 1741-, Year 2003
Publish dateMar 31, 2003 (structure data deposition date)
AuthorsErskine, P.T. / Coates, L. / Mall, S. / Gill, R.S. / Wood, S.P. / Myles, D.A.A. / Cooper, J.B.
External linksProtein Sci. / PubMed:12876323
MethodsX-ray diffraction
Resolution0.9 - 1.1 Å
Structure data

PDB-1oew:
ATOMIC RESOLUTION STRUCTURE OF NATIVE ENDOTHIAPEPSIN
Method: X-RAY DIFFRACTION / Resolution: 0.9 Å

PDB-1oex:
Atomic Resolution Structure of Endothiapepsin in Complex with a Hydroxyethylene Transition State Analogue Inhibitor H261
Method: X-RAY DIFFRACTION / Resolution: 1.1 Å

Chemicals

ChemComp-SER:
SERINE

ChemComp-THR:
THREONINE

ChemComp-GOL:
GLYCEROL

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

Source
  • cryphonectria parasitica (chestnut blight fungus)
  • synthetic construct (others)
KeywordsHYDROLASE / ASPARTIC PROTEINASE MECHANISM / ATOMIC RESOLUTION / SUCCINIMIDE / ANISOTROPIC REFINEMENT / HYDROLASE/HYDROLASE INHIBITOR / HYDROLASE-HYDROLASE INHIBITOR COMPLEX

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