1SBW

CRYSTAL STRUCTURE OF MUNG BEAN INHIBITOR LYSINE ACTIVE FRAGMENT COMPLEX WITH BOVINE BETA-TRYPSIN AT 1.8A RESOLUTION

1SBW の概要

• エントリーDOI: 10.2210/pdb1sbw/pdb
• 分子名称: PROTEIN (BETA-TRYPSIN), PROTEIN (MUNG BEAN INHIBITOR LYSIN ACTIVE FRAGMENT), CALCIUM ION, ... (5 entities in total)
• 機能のキーワード: complex(proteinase-inhibitor), hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• 由来する生物種: Bos taurus (cattle); 詳細
• 細胞内の位置: Secreted, extracellular space: P00760
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 27407.07

構造登録者

Huang, Q.,Zhu, Y.,Chi, C.,Tang, Y. (登録日: 1999-04-29, 公開日: 1999-05-06, 最終更新日: 2024-11-20)

主引用文献

Zhu, Y.,Huang, Q.,Chi, C.
Crystal structure of mung bean inhibitor lysine active fragment complex with bovine beta-trypsin at 1.8A resolution.
J.Biomol.Struct.Dyn., 16:1219-1224, 1999

PubMed Abstract: The crystal structure of the complex of mung bean inhibitor lysine active fragment with bovine beta-trypsin has been determined by X-ray crystallographic analysis at a resolution of 1.8 A. Refinement of the model of the complex converged at a final R value of 0.16. From the resulting electron density map, about one-third of the residues of the inhibitor were identified and two residues, at position P4 and P2' respectively, were found to be inconsistent with the sequence reported previously. The peptide chain of the inhibitor at the trypsin active site turns back sharply at Pro23I and forms a 9-residue reactive loop, which interacts with trypsin in a similar manner to the other families of inhibitors, suggesting an important and common role of these regions in exhibiting inhibitory activity.

PubMed: 10447205

実験手法

X-RAY DIFFRACTION (1.8 Å)