5AGY
CRYSTAL STRUCTURE OF A TAU CLASS GST MUTANT FROM GLYCINE
5AGY の概要
エントリーDOI | 10.2210/pdb5agy/pdb |
分子名称 | GLUTATHIONE S-TRANSFERASE, 4-NITROPHENYL METHANETHIOL, S-(P-NITROBENZYL)GLUTATHIONE, ... (5 entities in total) |
機能のキーワード | transferase, binding site, catalytic domain, enzyme, induction, detoxification, herbicides, kinetics, site-directed mutagenesis, soy beans, glutathione transferase, protein stability, catalytic mechanism, xenobiotic binding, allosterism |
由来する生物種 | GLYCINE MAX (SOYBEAN) |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 52696.64 |
構造登録者 | Axarli, I.,Muleta, A.W.,Vlachakis, D.,Kossida, S.,Kotzia, G.,Dhavala, P.,Papageorgiou, A.C.,Labrou, N.E. (登録日: 2015-02-04, 公開日: 2015-12-16, 最終更新日: 2024-01-10) |
主引用文献 | Axarli, I.,Muleta, A.W.,Vlachakis, D.,Kossida, S.,Kotzia, G.,Maltezos, A.,Dhavala, P.,Papageorgiou, A.C.,Labrou, N.E. Directed Evolution of Tau Class Glutathione Transferases Reveals a Site that Regulates Catalytic Efficiency and Masks Cooperativity. Biochem.J., 473:559-, 2016 Cited by PubMed: 26637269DOI: 10.1042/BJ20150930 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.75 Å) |
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