1MMO
CRYSTAL STRUCTURE OF A BACTERIAL NON-HAEM IRON HYDROXYLASE THAT CATALYSES THE BIOLOGICAL OXIDATION OF METHANE
1MMO の概要
| エントリーDOI | 10.2210/pdb1mmo/pdb |
| 分子名称 | METHANE MONOOXYGENASE HYDROLASE (BETA CHAIN), METHANE MONOOXYGENASE HYDROLASE (ALPHA CHAIN), METHANE MONOOXYGENASE HYDROLASE (GAMMA CHAIN), ... (6 entities in total) |
| 機能のキーワード | oxidoreductase (monooxygenase) |
| 由来する生物種 | Methylococcus capsulatus 詳細 |
| タンパク質・核酸の鎖数 | 6 |
| 化学式量合計 | 245693.23 |
| 構造登録者 | Rosenzweig, A.C.,Frederick, C.A.,Lippard, S.J.,Nordlund, P. (登録日: 1994-02-22, 公開日: 1995-02-27, 最終更新日: 2024-02-14) |
| 主引用文献 | Rosenzweig, A.C.,Frederick, C.A.,Lippard, S.J.,Nordlund, P. Crystal structure of a bacterial non-haem iron hydroxylase that catalyses the biological oxidation of methane. Nature, 366:537-543, 1993 Cited by PubMed Abstract: The 2.2 A crystal structure of the 251K alpha 2 beta 2 gamma 2 dimeric hydroxylase protein of methane monooxygenase from Methylococcus capsulatus (Bath) reveals the geometry of the catalytic di-iron core. The two iron atoms are bridged by exogenous hydroxide and acetate ligands and further coordinated by four glutamate residues, two histidine residues and a water molecule. The dinuclear iron centre lies in a hydrophobic active-site cavity for binding methane. An extended canyon runs between alpha beta pairs, which have many long alpha-helices, for possible docking of the reductase and coupling proteins required for catalysis. PubMed: 8255292DOI: 10.1038/366537a0 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.2 Å) |
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