1AK1
FERROCHELATASE FROM BACILLUS SUBTILIS
1AK1 の概要
| エントリーDOI | 10.2210/pdb1ak1/pdb |
| 分子名称 | FERROCHELATASE (2 entities in total) |
| 機能のキーワード | protoheme ferro-lyase, heme synthesis, porphyrin, metallation, b. subtilis |
| 由来する生物種 | Bacillus subtilis |
| 細胞内の位置 | Cytoplasm: P32396 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 35389.71 |
| 構造登録者 | Al-Karadaghi, S.,Hansson, M.,Nikonov, S.,Jonsson, B.,Hederstedt, L. (登録日: 1997-05-28, 公開日: 1997-12-03, 最終更新日: 2024-02-07) |
| 主引用文献 | Al-Karadaghi, S.,Hansson, M.,Nikonov, S.,Jonsson, B.,Hederstedt, L. Crystal structure of ferrochelatase: the terminal enzyme in heme biosynthesis. Structure, 5:1501-1510, 1997 Cited by PubMed Abstract: The metallation of closed ring tetrapyrroles resulting in the formation of hemes, chlorophylls and vitamin B12 is catalyzed by specific enzymes called chelatases. Ferrochelatase catalyzes the terminal step in heme biosynthesis by inserting ferrous ion into protoporphyrin IX by a mechanism that is poorly understood. Mutations in the human gene for ferrochelatase can result in the disease erythropoietic protoporphyria, and a further understanding of the mechanism of this enzyme is therefore of clinical interest. No three-dimensional structure of a tetrapyrrole metallation enzyme has been available until now. PubMed: 9384565DOI: 10.1016/S0969-2126(97)00299-2 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.9 Å) |
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