4LRS
Crystal and solution structures of the bifunctional enzyme (Aldolase/Aldehyde dehydrogenase) from Thermomonospora curvata, reveal a cofactor-binding domain motion during NAD+ and CoA accommodation whithin the shared cofactor-binding site
4LRS の概要
| エントリーDOI | 10.2210/pdb4lrs/pdb |
| 関連するPDBエントリー | 4LRT |
| 分子名称 | 4-hydroxy-2-oxovalerate aldolase, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, FORMYL GROUP, ... (12 entities in total) |
| 機能のキーワード | rossmann fold, tim barrel domain, dehydrogenase, aldolase, oxidoreductase |
| 由来する生物種 | Thermomonospora curvata 詳細 |
| タンパク質・核酸の鎖数 | 3 |
| 化学式量合計 | 73954.12 |
| 構造登録者 | Fischer, B.,Branlant, G.,Talfournier, F.,Gruez, A. (登録日: 2013-07-20, 公開日: 2013-09-04, 最終更新日: 2023-11-15) |
| 主引用文献 | Fischer, B.,Branlant, G.,Talfournier, F.,Gruez, A. Crystal and solution structures of the bifunctional enzyme (Aldolase/Aldehyde dehydrogenase) from Thermomonospora curvata, reveal a cofactor-binding domain motion during NAD+ and CoA accommodation whithin the shared cofactor-binding site To be Published, |
| 実験手法 | X-RAY DIFFRACTION (1.55 Å) |
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