1PIP
CRYSTAL STRUCTURE OF PAPAIN-SUCCINYL-GLN-VAL-VAL-ALA-ALA-P-NITROANILIDE COMPLEX AT 1.7 ANGSTROMS RESOLUTION: NONCOVALENT BINDING MODE OF A COMMON SEQUENCE OF ENDOGENOUS THIOL PROTEASE INHIBITORS
Summary for 1PIP
Entry DOI | 10.2210/pdb1pip/pdb |
Related PRD ID | PRD_000354 |
Descriptor | Papain, SUCCINYL-GLN-VAL-VAL-ALA-ALA-P-NITROANILIDE (2 entities in total) |
Functional Keywords | thiol protease, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor |
Biological source | Carica papaya (papaya) More |
Total number of polymer chains | 2 |
Total formula weight | 24156.09 |
Authors | Yamamoto, A.,Tomoo, K.,Doi, M.,Ohishi, H.,Inoue, M.,Ishida, T.,Yamamoto, D.,Tsuboi, S.,Okamoto, H.,Okada, Y. (deposition date: 1992-10-03, release date: 1993-10-31, Last modification date: 2024-04-24) |
Primary citation | Yamamoto, A.,Tomoo, K.,Doi, M.,Ohishi, H.,Inoue, M.,Ishida, T.,Yamamoto, D.,Tsuboi, S.,Okamoto, H.,Okada, Y. Crystal structure of papain-succinyl-Gln-Val-Val-Ala-Ala-p-nitroanilide complex at 1.7-A resolution: noncovalent binding mode of a common sequence of endogenous thiol protease inhibitors. Biochemistry, 31:11305-11309, 1992 Cited by PubMed: 1445868DOI: 10.1021/bi00161a007 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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