1AKD

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

Summary for 1AKD

• Entry DOI: 10.2210/pdb1akd/pdb
• Descriptor: CYTOCHROME P450CAM, POTASSIUM ION, PROTOPORPHYRIN IX CONTAINING FE, ... (5 entities in total)
• Functional Keywords: oxidoreductase, oxygenase, cytochrome p450, monooxygenase, electron transport
• Biological source: Pseudomonas putida
• Cellular location: Cytoplasm (By similarity): P00183
• Total number of polymer chains: 1
• Total formula weight: 47395.71

Authors

Schlichting, I.,Jung, C.,Schulze, H. (deposition date: 1997-05-16, release date: 1997-11-19, Last modification date: 2024-04-03)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.8 Å)