1GOI
Crystal structure of the D140N mutant of chitinase B from Serratia marcescens at 1.45 A resolution
1GOI の概要
| エントリーDOI | 10.2210/pdb1goi/pdb |
| 関連するPDBエントリー | 1E15 1E6N 1E6P 1E6R 1E6Z |
| 分子名称 | CHITINASE B, GLYCEROL, SULFATE ION, ... (4 entities in total) |
| 機能のキーワード | chitin degradation, hydrolase, glycosidase |
| 由来する生物種 | SERRATIA MARCESCENS |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 112523.43 |
| 構造登録者 | Kolstad, G.,Synstad, B.,Eijsink, V.G.H.,Van Aalten, D.M.F. (登録日: 2001-10-21, 公開日: 2001-11-15, 最終更新日: 2024-10-23) |
| 主引用文献 | Kolstad, G.,Synstad, B.,Eijsink, V.G.H.,Van Aalten, D.M.F. Structure of the D140N Mutant of Chitinase B from Serratia Marcescens at 1.45 A Resolution. Acta Crystallogr.,Sect.D, 58:377-, 2002 Cited by PubMed Abstract: The crystal structure of the inactive D140N mutant of Serratia marcescens was refined to 1.45 A resolution. The structure of the mutant was essentially identical to that of the wild type, with the exception of a rotation of Asp142 in the catalytic centre. In the mutant, this residue interacts with the catalytic acid (Glu144) and not with residue 140 as in the wild type. Thus, the 500-fold decrease in activity in the D140N mutant seems to be largely mediated by an effect on Asp142, confirming the crucial role of the latter residue in catalysis. PubMed: 11807282DOI: 10.1107/S0907444901018972 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.45 Å) |
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