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Structure paper

TitleX-ray analyses of aspartic proteinases. The three-dimensional structure at 2.1 A resolution of endothiapepsin.
Journal, issue, pagesJ. Mol. Biol., Vol. 211, Page 919-941, Year 1990
Publish dateMar 11, 1992 (structure data deposition date)
AuthorsBlundell, T.L. / Jenkins, J.A. / Sewell, B.T. / Pearl, L.H. / Cooper, J.B. / Tickle, I.J. / Veerapandian, B. / Wood, S.P.
External linksJ. Mol. Biol. / PubMed:2179568
MethodsX-ray diffraction
Resolution1.9 Å
Structure data

PDB-1ent:
X-RAY ANALYSES OF ASPARTIC PROTEINASES. THE THREE-DIMENSIONAL STRUCTURE AT 2.1 ANGSTROMS RESOLUTION OF ENDOTHIAPEPSIN
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

Chemicals

ChemComp-0EM:
N-(tert-butoxycarbonyl)-L-phenylalanyl-N-{(1S)-1-[(R)-hydroxy(2-{[(2S)-2-methylbutyl]amino}-2-oxoethyl)phosphoryl]-3-methylbutyl}-3-(1H-imidazol-3-ium-4-yl)-L-alaninamide

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

Source
  • cryphonectria parasitica (chestnut blight fungus)
KeywordsHYDROLASE/HYDROLASE INHIBITOR / ACID PROTEINASE / HYDROLASE-HYDROLASE INHIBITOR COMPLEX

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