1akd: Difference between revisions

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[[Image:1akd.gif|left|200px]]
{{Seed}}
[[Image:1akd.png|left|200px]]


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{{STRUCTURE_1akd|  PDB=1akd  |  SCENE=  }}  
{{STRUCTURE_1akd|  PDB=1akd  |  SCENE=  }}  


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




==Overview==
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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.
The line below this paragraph, {{ABSTRACT_PUBMED_9357977}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 9357977 is the PubMed ID number.
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{{ABSTRACT_PUBMED_9357977}}


==About this Structure==
==About this Structure==
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[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]
[[Category: Oxygenase]]
[[Category: Oxygenase]]
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