4CHA

STRUCTURE OF ALPHA-*CHYMOTRYPSIN REFINED AT 1.68 ANGSTROMS RESOLUTION

4CHA の概要

• エントリーDOI: 10.2210/pdb4cha/pdb
• 分子名称: ALPHA-CHYMOTRYPSIN A, ... (4 entities in total)
• 機能のキーワード: hydrolase (serine proteinase)
• 由来する生物種: Bos taurus (cattle); 詳細
• 細胞内の位置: Secreted, extracellular space: P00766 P00766 P00766
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 50525.12

構造登録者

Tsukada, H.,Blow, D.M. (登録日: 1984-11-26, 公開日: 1985-04-01, 最終更新日: 2024-10-23)

主引用文献

Tsukada, H.,Blow, D.M.
Structure of alpha-chymotrypsin refined at 1.68 A resolution.
J.Mol.Biol., 184:703-711, 1985

PubMed Abstract: Diffraction data for alpha-chymotrypsin crystals at -10 degrees C were measured at 1.68 A resolution and refined by restrained structure-factor least-squares refinement. The two independent chymotrypsin molecules in the crystallographic asymmetric unit were refined independently. The overall structure of alpha-chymotrypsin is little changed from published co-ordinates. The root-mean-square shift of C alpha co-ordinates is 0.42 A, co-ordinates for the two molecules showing a root-mean-square difference of 0.19 A. Certain regions with high disorder (residues 9 to 14, 73 to 79) remain difficult to interpret and several side-chains are disordered. Some water molecule positions have been changed. The absence of the tosyl group has made a significant difference to the refined structure at the active site. This now agrees closely with other enzymes of the trypsin family that have been refined at high resolution. There is a strong hydrogen bond between N epsilon 2 (His57) and O gamma (Ser195) in the free enzyme, in line with the published description of the charge relay system.

PubMed: 4046030
DOI: 10.1016/0022-2836(85)90314-6

実験手法

X-RAY DIFFRACTION (1.68 Å)