131L
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
131L の概要
エントリーDOI | 10.2210/pdb131l/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 | 18841.51 |
構造登録者 | |
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 Cited by PubMed: 8298466主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.7 Å) |
構造検証レポート
検証レポート(詳細版)をダウンロード