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1AK1

FERROCHELATASE FROM BACILLUS SUBTILIS

1AK1 の概要
エントリーDOI10.2210/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: 9384565
DOI: 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)
構造検証レポート
Validation report summary of 1ak1
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2025-12-31に公開中

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