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7LY8

The internal aldimine form of the wild-type Salmonella Typhimurium Tryptophan Synthase in complex with two molecules of N-(4'-trifluoromethoxybenzoyl)-2-amino-1-ethylphosphate (F6F) inhibitor at the enzyme alpha-site, a single F6F molecule at the enzyme beta-site, and sodium ion at the metal coordination site at 1.55 Angstrom resolution. One of the beta-Q114 rotamer conformations allows a hydrogen bond to form with the PLP oxygen at the position 3 in the ring

7LY8 の概要
エントリーDOI10.2210/pdb7ly8/pdb
関連するPDBエントリー4KKX 4WX2 4Y6G 4ZQC 5BW6 7KU9
分子名称Tryptophan synthase alpha chain, Tryptophan synthase beta chain, 2-{[4-(TRIFLUOROMETHOXY)BENZOYL]AMINO}ETHYL DIHYDROGEN PHOSPHATE, ... (9 entities in total)
機能のキーワードinhibitor, internal aldimine, lyase, lyase-lyase inhibitor complex, lyase/lyase inhibitor
由来する生物種Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
詳細
タンパク質・核酸の鎖数2
化学式量合計73406.96
構造登録者
Hilario, E.,Dunn, M.F.,Mueller, L.J. (登録日: 2021-03-06, 公開日: 2022-03-09, 最終更新日: 2023-10-18)
主引用文献Hilario, E.,Dunn, M.F.,Mueller, L.J.
The internal aldimine form of the wild-type Salmonella Typhimurium Tryptophan Synthase in complex with two molecules of N-(4'-trifluoromethoxybenzoyl)-2-amino-1-ethylphosphate (F6F) inhibitor at the enzyme alpha-site, a single F6F molecule at the enzyme beta-site, and sodium ion at the metal coordination site at 1.55 Angstrom resolution. One of the beta-Q114 rotamer conformations allows a hydrogen bond to form with the PLP oxygen at the position 3 in the ring.
To be Published,
実験手法
X-RAY DIFFRACTION (1.55 Å)
構造検証レポート
Validation report summary of 7ly8
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-15に公開中

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