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: 1445868 DOI: 10.1021/bi00161a007 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.7 Å)

Structure validation