1BP4
USE OF PAPAIN AS A MODEL FOR THE STRUCTURE-BASED DESIGN OF CATHEPSIN K INHIBITORS. CRYSTAL STRUCTURES OF TWO PAPAIN INHIBITOR COMPLEXES DEMONSTRATE BINDING TO S'-SUBSITES.
Summary for 1BP4
Entry DOI | 10.2210/pdb1bp4/pdb |
Related PRD ID | PRD_001210 |
Descriptor | PAPAIN, N-[(benzyloxy)carbonyl]-L-leucyl-N-[(2S)-1-hydroxy-4-methylpentan-2-yl]-L-leucinamide (3 entities in total) |
Functional Keywords | hydrolase, sulfhydryl proteinase |
Biological source | Carica papaya (papaya) |
Total number of polymer chains | 1 |
Total formula weight | 23926.98 |
Authors | Lalonde, J.M.,Zhao, B.,Smith, W.W.,Janson, C.A.,Desjarlais, R.L.,Tomaszek, T.A.,Carr, T.J.,Thompson, S.K.,Yamashita, D.S.,Veber, D.F.,Abdel-Mequid, S.S. (deposition date: 1998-08-12, release date: 1999-08-12, Last modification date: 2023-08-09) |
Primary citation | LaLonde, J.M.,Zhao, B.,Smith, W.W.,Janson, C.A.,DesJarlais, R.L.,Tomaszek, T.A.,Carr, T.J.,Thompson, S.K.,Oh, H.J.,Yamashita, D.S.,Veber, D.F.,Abdel-Meguid, S.S. Use of papain as a model for the structure-based design of cathepsin K inhibitors: crystal structures of two papain-inhibitor complexes demonstrate binding to S'-subsites. J.Med.Chem., 41:4567-4576, 1998 Cited by PubMed: 9804696DOI: 10.1021/jm980249f PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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