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1A4I

HUMAN TETRAHYDROFOLATE DEHYDROGENASE / CYCLOHYDROLASE

1A4I の概要
エントリーDOI10.2210/pdb1a4i/pdb
分子名称METHYLENETETRAHYDROFOLATE DEHYDROGENASE / METHENYLTETRAHYDROFOLATE CYCLOHYDROLASE, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE (3 entities in total)
機能のキーワードthf, bifunctional, dehydrogenase, cyclohydrolase, folate, oxidoreductase
由来する生物種Homo sapiens (human)
細胞内の位置Cytoplasm: P11586
タンパク質・核酸の鎖数2
化学式量合計66791.93
構造登録者
Allaire, M.,Li, Y.,Mackenzie, R.E.,Cygler, M. (登録日: 1998-01-30, 公開日: 1999-02-09, 最終更新日: 2024-02-07)
主引用文献Allaire, M.,Li, Y.,MacKenzie, R.E.,Cygler, M.
The 3-D structure of a folate-dependent dehydrogenase/cyclohydrolase bifunctional enzyme at 1.5 A resolution.
Structure, 6:173-182, 1998
Cited by
PubMed Abstract: The interconversion of two major folate one-carbon donors occurs through the sequential activities of NAD(P)-dependent methylene[H4]folate dehydrogenase (D) and methenyl[H4]folate cyclohydrolase (C). These activities often coexist as part of a multifunctional enzyme and there are several lines of evidence suggesting that their substrates bind at overlapping sites. Little is known, however, about the nature of this site or the identity of the active-site residues for this enzyme family.
PubMed: 9519408
DOI: 10.1016/S0969-2126(98)00019-7
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.5 Å)
構造検証レポート
Validation report summary of 1a4i
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2025-12-31に公開中

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