2CEQ
Beta-glycosidase from Sulfolobus solfataricus in complex with glucoimidazole
2CEQ の概要
エントリーDOI | 10.2210/pdb2ceq/pdb |
関連するPDBエントリー | 1GOW 1UWI 1UWQ 1UWR 1UWS 1UWT 1UWU 2CER |
分子名称 | BETA-GALACTOSIDASE, ACETATE ION, GLUCOIMIDAZOLE, ... (4 entities in total) |
機能のキーワード | archaeon, family 1, glycoside hydrolase, glucoimidazole, glycosidase, hydrolase |
由来する生物種 | SULFOLOBUS SOLFATARICUS |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 114216.41 |
構造登録者 | Gloster, T.M.,Moracci, M.,Vasella, A.,Davies, G.J. (登録日: 2006-02-10, 公開日: 2006-09-27, 最終更新日: 2023-12-13) |
主引用文献 | Gloster, T.M.,Roberts, S.,Perugino, G.,Rossi, M.,Moracci, M.,Panday, N.,Terinek, M.,Vasella, A.,Davies, G.J. Structural, Kinetic, and Thermodynamic Analysis of Glucoimidazole-Derived Glycosidase Inhibitors. Biochemistry, 45:11879-, 2006 Cited by PubMed Abstract: Inhibition of glycosidases has great potential in the quest for highly potent and specific drugs to treat diseases such as diabetes, cancer, and viral infections. One of the most effective ways of designing such compounds is by mimicking the transition state. Here we describe the structural, kinetic, and thermodynamic dissection of binding of two glucoimidazole-derived compounds, which are among the most potent glycosidase inhibitors reported to date, with two family 1 beta-glycosidases. Provocatively, while inclusion of the phenethyl moiety improves binding by a factor of 20-80-fold, this does not appear to result from better noncovalent interactions with the enzyme; instead, improved affinity may be derived from significantly better entropic contributions to binding displayed by the phenethyl-substituted imidazole compound. PubMed: 17002288DOI: 10.1021/BI060973X 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.14 Å) |
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