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
收藏Protein Data Bank Japan2024-11-13 更新2026-03-21 收录
下载链接：
https://pdbj.org/mine/summary/1pip
下载链接
链接失效反馈官方服务：
资源简介：
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 Descriptor: Papain, SUCCINYL-GLN-VAL-VAL-ALA-ALA-P-NITROANILIDE Authors: Yamamoto, A, Tomoo, K, Doi, M, Ohishi, H, Inoue, M, Ishida, T, Yamamoto, D, Tsuboi, S, Okamoto, H, Okada, Y. Deposit date: 1992-10-03 Release date: 1993-10-31 Last modified: 2024-11-13 Method: X-RAY DIFFRACTION (1.7 Å) Cite: 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, 1992
创建时间：
1992-10-03
