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1B9L

7,8-DIHYDRONEOPTERIN TRIPHOSPHATE EPIMERASE

1B9L の概要
エントリーDOI10.2210/pdb1b9l/pdb
分子名称PROTEIN (EPIMERASE) (1 entity in total)
機能のキーワードepimerase, isomerase
由来する生物種Escherichia coli
タンパク質・核酸の鎖数8
化学式量合計112824.19
構造登録者
Ploom, T.,Haussmann, C.,Hof, P.,Steinbacher, S.,Bacher, A.,Richardson, J.,Huber, R. (登録日: 1999-02-11, 公開日: 2000-02-18, 最終更新日: 2023-12-27)
主引用文献Ploom, T.,Haussmann, C.,Hof, P.,Steinbacher, S.,Bacher, A.,Richardson, J.,Huber, R.
Crystal structure of 7,8-dihydroneopterin triphosphate epimerase.
Structure Fold.Des., 7:509-516, 1999
Cited by
PubMed Abstract: Dihydroneopterin triphosphate (H2NTP) is the central substrate in the biosynthesis of folate and tetrahydrobiopterin. Folate serves as a cofactor in amino acid and purine biosynthesis and tetrahydrobiopterin is used as a cofactor in amino acid hydroxylation and nitric oxide synthesis. In bacteria, H2NTP enters the folate biosynthetic pathway after nonenzymatic dephosphorylation; in vertebrates, H2NTP is used to synthesize tetrahydrobiopterin. The dihydroneopterin triphosphate epimerase of Escherichia coli catalyzes the inversion of carbon 2' of H2NTP.
PubMed: 10378270
DOI: 10.1016/S0969-2126(99)80067-7
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.9 Å)
構造検証レポート
Validation report summary of 1b9l
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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