1R26
Crystal structure of thioredoxin from Trypanosoma brucei brucei
1R26 の概要
| エントリーDOI | 10.2210/pdb1r26/pdb |
| 分子名称 | Thioredoxin (2 entities in total) |
| 機能のキーワード | redox-active disulfide; thioredoxin, electron transport |
| 由来する生物種 | Trypanosoma |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 14483.93 |
| 構造登録者 | Friemann, R.,Schmidt, H.,Ramaswamy, S.,Forstner, M.,Krauth-Siegel, R.L.,Eklund, H. (登録日: 2003-09-26, 公開日: 2003-12-09, 最終更新日: 2024-11-06) |
| 主引用文献 | Friemann, R.,Schmidt, H.,Ramaswamy, S.,Forstner, M.,Krauth-Siegel, R.L.,Eklund, H. Structure of thioredoxin from Trypanosoma brucei brucei FEBS Lett., 554:301-305, 2003 Cited by PubMed Abstract: The three-dimensional structure of thioredoxin from Trypanosoma brucei brucei has been determined at 1.4 A resolution. The overall structure is more similar to that of human thioredoxin than to any other thioredoxin structure. The most striking difference to other thioredoxins is the absence of a buried carboxylate behind the active site cysteines. Instead of the common Asp, there is a Trp that binds an ordered water molecule probably involved in the protonation/deprotonation of the more buried cysteine during catalysis. The conserved Trp in the WCGPC sequence motif has an exposed position that can interact with target proteins. PubMed: 14623083DOI: 10.1016/S0014-5793(03)01173-6 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.4 Å) |
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