1EXP
BETA-1,4-GLYCANASE CEX-CD
1EXP の概要
| エントリーDOI | 10.2210/pdb1exp/pdb |
| 関連するBIRD辞書のPRD_ID | PRD_900050 |
| 分子名称 | BETA-1,4-D-GLYCANASE CEX-CD, beta-D-glucopyranose-(1-4)-2-deoxy-2-fluoro-alpha-D-glucopyranose (3 entities in total) |
| 機能のキーワード | cellulose degradation, hydrolase, glycosidase |
| 由来する生物種 | Cellulomonas fimi |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 34396.23 |
| 構造登録者 | White, A.,Tull, D.,Johns, K.L.,Withers, S.G.,Rose, D.R. (登録日: 1996-01-11, 公開日: 1997-01-27, 最終更新日: 2024-11-06) |
| 主引用文献 | White, A.,Tull, D.,Johns, K.,Withers, S.G.,Rose, D.R. Crystallographic observation of a covalent catalytic intermediate in a beta-glycosidase. Nat.Struct.Biol., 3:149-154, 1996 Cited by PubMed Abstract: The three-dimensional structure of a catalytically competent glycosyl-enzyme intermediate of a retaining beta-1,4-glycanase has been determined at a resolution of 1.8 A by X-ray diffraction. A fluorinated slow substrate forms an alpha-D-glycopyranosyl linkage to one of the two invariant carboxylates, Glu 233, as supported in solution by 19F-NMR studies. The resulting ester linkage is coplanar with the cyclic oxygen of the proximal saccharide and is inferred to form a strong hydrogen bond with the 2-hydroxyl of that saccharide unit in natural substrates. The active-site architecture of this covalent intermediate gives insights into both the classical double-displacement catalytic mechanism and the basis for the enzyme's specificity. PubMed: 8564541DOI: 10.1038/nsb0296-149 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.8 Å) |
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