1EPP
ENDOTHIA ASPARTIC PROTEINASE (ENDOTHIAPEPSIN) COMPLEXED WITH PD-130,693 (MAS PHE LYS+MTF STA MBA)
Summary for 1EPP
Entry DOI | 10.2210/pdb1epp/pdb |
Related | 1EPQ |
Related PRD ID | PRD_000392 |
Descriptor | ENDOTHIAPEPSIN, SULFATE ION, N-(dimethylsulfamoyl)-L-phenylalanyl-N-[(1S,2S)-2-hydroxy-4-{[(2S)-2-methylbutyl]amino}-1-(2-methylpropyl)-4-oxobutyl]-N~6~-(methylcarbamothioyl)-L-lysinamide, ... (4 entities in total) |
Functional Keywords | hydrolase-hydrolase inhibitor complex, acid proteinase, hydrolase/hydrolase inhibitor |
Biological source | Cryphonectria parasitica (chestnut blight fungus) |
Total number of polymer chains | 1 |
Total formula weight | 34705.95 |
Authors | Wallace, B.A.,Cooper, J.B.,Blundell, T.L. (deposition date: 1994-07-27, release date: 1994-12-20, Last modification date: 2017-11-29) |
Primary citation | Lunney, E.A.,Hamilton, H.W.,Hodges, J.C.,Kaltenbronn, J.S.,Repine, J.T.,Badasso, M.,Cooper, J.B.,Dealwis, C.,Wallace, B.A.,Lowther, W.T. Analyses of ligand binding in five endothiapepsin crystal complexes and their use in the design and evaluation of novel renin inhibitors. J.Med.Chem., 36:3809-3820, 1993 Cited by PubMed: 8254610DOI: 10.1021/jm00076a008 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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