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3MPG

Dihydroorotase from Bacillus anthracis

3MPG の概要
エントリーDOI10.2210/pdb3mpg/pdb
分子名称Dihydroorotase, ZINC ION (3 entities in total)
機能のキーワードhydrolase
由来する生物種Bacillus anthracis (anthrax)
タンパク質・核酸の鎖数2
化学式量合計93698.20
構造登録者
Santarsiero, B.D.,Mehboob, S.,Johnson, M.E. (登録日: 2010-04-26, 公開日: 2010-11-10, 最終更新日: 2024-02-21)
主引用文献Mehboob, S.,Mulhearn, D.C.,Truong, K.,Johnson, M.E.,Santarsiero, B.D.
Structure of dihydroorotase from Bacillus anthracis at 2.6A resolution.
Acta Crystallogr.,Sect.F, 66:1432-1435, 2010
Cited by
PubMed Abstract: Dihydroorotase (EC 3.5.2.3) catalyzes the reversible cyclization of N-carbamoyl-L-aspartate to L-dihydroorotate in the third step of the pyrimidine-biosynthesis pathway in Bacillus anthracis. A comparison is made between the structures of dihydroorotase from four different organisms, including B. anthracis dihydroorotase, and reveals substantial variations in the active site, dimer interface and overall tertiary structure. These differences demonstrate the utility of exploring multiple structures of a molecular target as expressed from different organisms and how these differences can be exploited for structure-based drug discovery.
PubMed: 21045288
DOI: 10.1107/S1744309110037085
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.6 Å)
構造検証レポート
Validation report summary of 3mpg
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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