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Structure paper

TitleThe Catalytic Mechanism of an Aspartic Proteinase Explored with Neutron and X-Ray Diffraction
Journal, issue, pagesJ. Am. Chem. Soc., Vol. 130, Page 7235-, Year 2008
Publish dateApr 9, 2008 (structure data deposition date)
AuthorsCoates, L. / Tuan, H.-F. / Tomanicek, S.J. / Kovalevsky, A. / Mustyakimov, M. / Erskine, P. / Cooper, J.
External linksJ. Am. Chem. Soc. / PubMed:18479128
MethodsX-ray diffraction / neutron diffraction
Resolution1 - 2 Å
Structure data

PDB-2jji:
Endothiapepsin in complex with a gem-diol inhibitor.
Method: X-RAY DIFFRACTION / Resolution: 1.57 Å

PDB-2jjj:
Endothiapepsin in complex with a gem-diol inhibitor.
Method: X-RAY DIFFRACTION / Resolution: 1 Å

PDB-2vs2:
Neutron diffraction structure of endothiapepsin in complex with a gem- diol inhibitor.
Method: NEUTRON DIFFRACTION / Resolution: 2 Å

Chemicals

ChemComp-0QS:
N~2~-[(2R)-2-benzyl-3-(tert-butylsulfonyl)propanoyl]-N-{(1R)-1-(cyclohexylmethyl)-3,3-difluoro-2,2-dihydroxy-4-[(2-morpholin-4-ylethyl)amino]-4-oxobutyl}-3-(1H-imidazol-3-ium-4-yl)-L-alaninamide

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

ChemComp-DOD:
DEUTERATED WATER

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

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