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2CFI

The hydrolase domain of human 10-FTHFD in complex with 6- formyltetrahydropterin

2CFI の概要
エントリーDOI10.2210/pdb2cfi/pdb
関連するPDBエントリー2BW0 2CQ8
分子名称10-FORMYLTETRAHYDROFOLATE DEHYDROGENASE, SULFATE ION, 6-FORMYLTETRAHYDROPTERIN, ... (4 entities in total)
機能のキーワードtetrahydrofolate, folate binding, nadp, one-carbon metabolism, oxidoreductase, phosphopantetheine
由来する生物種HOMO SAPIENS (HUMAN)
細胞内の位置Cytoplasm: O75891
タンパク質・核酸の鎖数1
化学式量合計36866.86
構造登録者
主引用文献Kursula, P.,Schuler, H.,Flodin, S.,Nilsson-Ehle, P.,Ogg, D.J.,Savitsky, P.,Nordlund, P.,Stenmark, P.
Structures of the Hydrolase Domain of Human 10-Formyltetrahydrofolate Dehydrogenase and its Complex with a Substrate Analogue.
Acta Crystallogr.,Sect.D, 62:1294-, 2006
Cited by
PubMed Abstract: 10-Formyltetrahydrofolate dehydrogenase is a ubiquitously expressed enzyme in the human body. It catalyses the formation of tetrahydrofolate and carbon dioxide from 10-formyltetrahydrofolate, thereby playing an important role in the human metabolism of one-carbon units. It is a two-domain protein in which the N-terminal domain hydrolyses 10-formyltetrahydrofolate into formate and tetrahydrofolate. The high-resolution crystal structure of the hydrolase domain from human 10-formyltetrahydrofolate dehydrogenase has been determined in the presence and absence of a substrate analogue. The structures reveal conformational changes of two loops upon ligand binding, while key active-site residues appear to be pre-organized for catalysis prior to substrate binding. Two water molecules in the structures mark the positions of key oxygen moieties in the catalytic reaction and reaction geometries are proposed based on the structural data.
PubMed: 17057331
DOI: 10.1107/S0907444906026849
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.85 Å)
構造検証レポート
Validation report summary of 2cfi
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2026-01-28に公開中

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