3MPG
Dihydroorotase from Bacillus anthracis
3MPG の概要
| エントリーDOI | 10.2210/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 | |
| 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: 21045288DOI: 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) |
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