129L

STRUCTURES OF RANDOMLY GENERATED MUTANTS OF T4 LYSOZYME SHOW THAT PROTEIN STABILITY CAN BE ENHANCED BY RELAXATION OF STRAIN AND BY IMPROVED HYDROGEN BONDING VIA BOUND SOLVENT

129L の概要

• エントリーDOI: 10.2210/pdb129l/pdb
• 分子名称: T4 LYSOZYME, CHLORIDE ION, BETA-MERCAPTOETHANOL, ... (4 entities in total)
• 機能のキーワード: hydrolase(o-glycosyl)
• 由来する生物種: Enterobacteria phage T4
• 細胞内の位置: Host cytoplasm : P00720
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 18885.56

構造登録者

Pjura, P.,Matthews, B.W. (登録日: 1993-05-28, 公開日: 1994-01-31, 最終更新日: 2024-02-07)

• 主引用文献: Pjura, P.,Matthews, B.W.; Structures of randomly generated mutants of T4 lysozyme show that protein stability can be enhanced by relaxation of strain and by improved hydrogen bonding via bound solvent.; Protein Sci., 2:2226-2232, 1993; PubMed: 8298466

実験手法

X-RAY DIFFRACTION (1.7 Å)