3HF2
Crystal structure of the I401P mutant of cytochrome P450 BM3
3HF2 の概要
| エントリーDOI | 10.2210/pdb3hf2/pdb |
| 分子名称 | Bifunctional P-450/NADPH-P450 reductase, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total) |
| 機能のキーワード | p450 family protein fold, oxidoreductase, electron transport, fad, flavoprotein, fmn, heme, iron, metal-binding, monooxygenase, multifunctional enzyme, nadp, transport |
| 由来する生物種 | Bacillus megaterium |
| 細胞内の位置 | Cytoplasm (By similarity): P14779 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 111244.26 |
| 構造登録者 | Yang, W.,Whitehouse, C.J.C.,Bell, S.G.,Bartlam, M.,Wong, L.L.,Rao, Z. (登録日: 2009-05-10, 公開日: 2009-06-30, 最終更新日: 2023-11-01) |
| 主引用文献 | Whitehouse, C.J.C.,Bell, S.G.,Yang, W.,Yorke, J.A.,Blanford, C.F.,Strong, A.J.F.,Morse, E.J.,Bartlam, M.,Rao, Z.,Wong, L.-L. A Highly Active Single-Mutation Variant of P450(BM3) (CYP102A1) Chembiochem, 10:1654-1656, 2009 Cited by PubMed Abstract: The power of proline: Bold amino acid substitutions in sensitive protein regions are frequently unproductive, while more subtle mutations can be sufficient to bring about dramatic changes. But introducing proline at the residue next to the sulfur ligand in P450(BM3) (CYP102A1) has the unexpected and desirable effect of enhancing the activity of this fatty acid hydroxylase with a broad range of non-natural substrates, as illustrated by the figure. PubMed: 19492389DOI: 10.1002/cbic.200900279 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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