Loading
PDBj
メニューPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

2FEU

P450CAM from Pseudomonas putida reconstituted with manganic protoporphyrin IX

2FEU の概要
エントリーDOI10.2210/pdb2feu/pdb
関連するPDBエントリー2FE6 2FER
分子名称Cytochrome P450-cam, POTASSIUM ION, PROTOPORPHYRIN IX CONTAINING MN, ... (6 entities in total)
機能のキーワードmono-oxygenase, heme, manganic, substrate-bound, oxidoreductase
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2
化学式量合計94718.64
構造登録者
von Koenig, K.,Makris, T.M.,Sligar, S.G.,Schlichting, I. (登録日: 2005-12-16, 公開日: 2006-03-14, 最終更新日: 2023-08-30)
主引用文献Makris, T.M.,von Koenig, K.,Schlichting, I.,Sligar, S.G.
The status of high-valent metal oxo complexes in the P450 cytochromes.
J.Inorg.Biochem., 100:507-518, 2006
Cited by
PubMed Abstract: The oxidative prowess of the P450 cytochromes in physiological reactions is attributed to the production of a high-valent iron-oxo complex, or Compound I intermediate, in the reaction cycle. Despite many years of study, however, the full electronic description of this fleeting intermediate still remains an active area of study. In this manuscript, the current status of the isolation and characterization of the P450 oxo-Fe(IV) is examined and compared to analogous states in related heme enzymes. In addition, the utilization of cofactor exchange to stabilize high-valent oxo-states in the P450 is addressed. Structural and spectroscopic studies on manganese reconstituted P450, and its corresponding oxo-complex, are presented.
PubMed: 16510191
DOI: 10.1016/j.jinorgbio.2006.01.025
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.7 Å)
構造検証レポート
Validation report summary of 2feu
検証レポート(詳細版)ダウンロードをダウンロード

250059

件を2026-03-04に公開中

PDB statisticsPDBj update infoContact PDBjnumon