2CPP の概要
| エントリーDOI | 10.2210/pdb2cpp/pdb |
| 分子名称 | CYTOCHROME P450-CAM, PROTOPORPHYRIN IX CONTAINING FE, CAMPHOR, ... (4 entities in total) |
| 機能のキーワード | oxidoreductase(oxygenase) |
| 由来する生物種 | Pseudomonas putida |
| 細胞内の位置 | Cytoplasm : P00183 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 47357.60 |
| 構造登録者 | |
| 主引用文献 | Poulos, T.L.,Finzel, B.C.,Howard, A.J. High-resolution crystal structure of cytochrome P450cam. J.Mol.Biol., 195:687-700, 1987 Cited by PubMed Abstract: The crystal structure of Pseudomonas putida cytochrome P450cam with its substrate, camphor, bound has been refined to R = 0.19 at a normal resolution of 1.63 A. While the 1.63 A model confirms our initial analysis based on the 2.6 A model, the higher resolution structure has revealed important new details. These include a more precise assignment of sequence to secondary structure, the identification of three cis-proline residues, and a more detailed picture of substrate-protein interactions. In addition, 204 ordered solvent molecules have been found, one of which appears to be a cation. The cation stabilizes an unfavorable polypeptide conformation involved in forming part of the active site pocket, suggesting that the cation may be the metal ion binding site associated with the well-known ability of metal ions to enhance formation of the enzyme-substrate complex. Another unusual polypeptide conformation forms the proposed oxygen-binding pocket. A localized distortion and widening of the distal helix provides a pocket for molecular oxygen. An intricate system of side-chain to backbone hydrogen bonds aids in stabilizing the required local disruption in helical geometry. Sequence homologies strongly suggest a common oxygen-binding pocket in all P450 species. Further sequence comparisons between P450 species indicate common three-dimensional structures with changes focused in a region of the molecule postulated to be associated with the control of substrate specificity. PubMed: 3656428DOI: 10.1016/0022-2836(87)90190-2 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.63 Å) |
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