1JFB
X-ray structure of nitric oxide reductase (cytochrome P450nor) in the ferric resting state at atomic resolution
1JFB の概要
| エントリーDOI | 10.2210/pdb1jfb/pdb |
| 関連するPDBエントリー | 1JFC |
| 分子名称 | nitric-oxide reductase cytochrome P450 55A1, PROTOPORPHYRIN IX CONTAINING FE, GLYCEROL, ... (4 entities in total) |
| 機能のキーワード | nitric oxide reductase, cytochrome p450nor, atomic resolution, riken structural genomics/proteomics initiative, rsgi, structural genomics, oxidoreductase |
| 由来する生物種 | Fusarium oxysporum |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 45230.37 |
| 構造登録者 | Shimizu, H.,Adachi, S.,Park, S.Y.,Shiro, Y.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (登録日: 2001-06-20, 公開日: 2001-12-20, 最終更新日: 2024-03-13) |
| 主引用文献 | Shimizu, H.,Park, S.Y.,Shiro, Y.,Adachi, S. X-ray structure of nitric oxide reductase (cytochrome P450nor) at atomic resolution. Acta Crystallogr.,Sect.D, 58:81-89, 2002 Cited by PubMed Abstract: Crystal structures of the nitric oxide reductase cytochrome P450nor (P450nor) in the ferric resting and the ferrous carbonmonoxy (CO) states have been determined at 1.00 and 1.05 A resolution, respectively. P450nor consists of 403 amino-acid residues (46 kDa) and is one of the largest proteins refined to this resolution so far. The final models have conventional R factors of 10.2% (ferric resting) and 11.7% (ferrous CO), with mean coordinate errors of 0.028 (ferric resting) and 0.030 A (ferrous CO) as calculated from inversion of the full positional least-squares matrix. Owing to the atomic resolution, novel features are found in the refined structures. Firstly, two orientations of the haem are observed both in the ferric resting and the ferrous CO states. Secondly, a disordered water molecule bound to the haem iron is found in the ferric resting state. In addition, the accurate structures at atomic resolution enabled the examination of general stereochemical parameters that are commonly used in refinement cycles of protein structures. PubMed: 11752781DOI: 10.1107/S0907444901017383 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1 Å) |
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