1AKD

CYTOCHROME P450CAM FROM PSEUDOMONAS PUTIDA, COMPLEXED WITH 1S-CAMPHOR

1AKD の概要

• エントリーDOI: 10.2210/pdb1akd/pdb
• 分子名称: CYTOCHROME P450CAM, POTASSIUM ION, PROTOPORPHYRIN IX CONTAINING FE, ... (5 entities in total)
• 機能のキーワード: oxidoreductase, oxygenase, cytochrome p450, monooxygenase, electron transport
• 由来する生物種: Pseudomonas putida
• 細胞内の位置: Cytoplasm (By similarity): P00183
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 47395.71

構造登録者

Schlichting, I.,Jung, C.,Schulze, H. (登録日: 1997-05-16, 公開日: 1997-11-19, 最終更新日: 2024-04-03)

主引用文献

Schlichting, I.,Jung, C.,Schulze, H.
Crystal structure of cytochrome P-450cam complexed with the (1S)-camphor enantiomer.
FEBS Lett., 415:253-257, 1997

PubMed Abstract: The crystal structure of cytochrome P-450cam complexed with the enantiomer (1S)-camphor has been solved to 1.8 angstroms resolution and compared with the structure of the (1R)-camphor P-450cam complex. The overall protein structure is the same for both enantiomer complexes. However, the orientation of the substrates in the heme pocket differs. In contrast to (1R)-camphor, the (1S)-enantiomer binds in at least two orientations. The major binding mode of (1S)-camphor resembles the one of the (1R)-enantiomer in that there is a hydrogen bond between Tyr-96 and the quinone group of camphor, and the 10-methyl group points towards the I-helix. The binding differs in that C-5 is not at a position suitable for hydroxylation. In the other orientation (1S)-camphor is not hydrogen bonded, but C-5 is located suitably for hydroxylation.

PubMed: 9357977
DOI: 10.1016/S0014-5793(97)01135-6

実験手法

X-RAY DIFFRACTION (1.8 Å)