5ER2
High-resolution X-ray diffraction study of the complex between endothiapepsin and an oligopeptide inhibitor. the analysis of the inhibitor binding and description of the rigid body shift in the enzyme
Summary for 5ER2
Entry DOI | 10.2210/pdb5er2/pdb |
Related PRD ID | PRD_000262 |
Descriptor | ENDOTHIAPEPSIN, 6-ammonio-N-{[(2R,3R)-3-{[N-(tert-butoxycarbonyl)-L-phenylalanyl-3-(1H-imidazol-3-ium-4-yl)-L-alanyl]amino}-4-cyclohexyl-2-hydroxybutyl](2-methylpropyl)carbamoyl}-L-norleucyl-L-phenylalanine (3 entities in total) |
Functional Keywords | acid proteinase, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor |
Biological source | Cryphonectria parasitica (chestnut blight fungus) |
Total number of polymer chains | 1 |
Total formula weight | 34762.06 |
Authors | Sali, A.,Veerapandian, B.,Cooper, J.B.,Foundling, S.I.,Hoover, D.J.,Blundell, T.L. (deposition date: 1991-01-02, release date: 1991-04-15, Last modification date: 2017-11-29) |
Primary citation | Sali, A.,Veerapandian, B.,Cooper, J.B.,Foundling, S.I.,Hoover, D.J.,Blundell, T.L. High-resolution X-ray diffraction study of the complex between endothiapepsin and an oligopeptide inhibitor: the analysis of the inhibitor binding and description of the rigid body shift in the enzyme. EMBO J., 8:2179-2188, 1989 Cited by PubMed: 2676515PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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