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1QD1

THE CRYSTAL STRUCTURE OF THE FORMIMINOTRANSFERASE DOMAIN OF FORMIMINOTRANSFERASE-CYCLODEAMINASE.

1QD1 の概要
エントリーDOI10.2210/pdb1qd1/pdb
分子名称FORMIMINOTRANSFERASE-CYCLODEAMINASE, N-{[4-({[(6R)-2-amino-5-formyl-4-oxo-1,4,5,6,7,8-hexahydropteridin-6-yl]methyl}amino)phenyl]carbonyl}-L-glutamic acid, GLYCEROL, ... (4 entities in total)
機能のキーワードfunctional dimer, alpha-beta-beta-alpha sandwich, electrostatically charged substrate tunnel, transferase
由来する生物種Sus scrofa (pig)
細胞内の位置Cytoplasm, cytoskeleton, centrosome, centriole (By similarity): P53603
タンパク質・核酸の鎖数2
化学式量合計72888.89
構造登録者
Kohls, D.,Sulea, T.,Purisima, E.,MacKenzie, R.E.,Vrielink, A. (登録日: 1999-07-08, 公開日: 2000-01-12, 最終更新日: 2024-02-14)
主引用文献Kohls, D.,Sulea, T.,Purisima, E.O.,MacKenzie, R.E.,Vrielink, A.
The crystal structure of the formiminotransferase domain of formiminotransferase-cyclodeaminase: implications for substrate channeling in a bifunctional enzyme.
Structure Fold.Des., 8:35-46, 2000
Cited by
PubMed Abstract: The bifunctional enzyme formiminotransferase-cyclodeaminase (FTCD) contains two active sites at different positions on the protein structure. The enzyme binds a gamma-linked polyglutamylated form of the tetrahydrofolate substrate and channels the product of the transferase reaction from the transferase active site to the cyclodeaminase active site. Structural studies of this bifunctional enzyme and its monofunctional domains will provide insight into the mechanism of substrate channeling and the two catalytic reactions.
PubMed: 10673422
DOI: 10.1016/S0969-2126(00)00078-2
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.7 Å)
構造検証レポート
Validation report summary of 1qd1
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2026-04-22に公開中

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