3m4v: Difference between revisions

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{{STRUCTURE_3m4v|  PDB=3m4v  |  SCENE=  }}  
{{STRUCTURE_3m4v|  PDB=3m4v  |  SCENE=  }}  
===Crystal structure of the A330P mutant of cytochrome P450 BM3===
===Crystal structure of the A330P mutant of cytochrome P450 BM3===
{{ABSTRACT_PUBMED_21110374}}


==Function==
==Function==
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==About this Structure==
==About this Structure==
[[3m4v]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_megaterium Bacillus megaterium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M4V OCA].  
[[3m4v]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_14581 Atcc 14581]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M4V OCA].  


==See Also==
==See Also==
*[[Cytochrome P450|Cytochrome P450]]
*[[Cytochrome P450|Cytochrome P450]]
[[Category: Bacillus megaterium]]
*[[NADPH-Cytochrome P450 Reductase|NADPH-Cytochrome P450 Reductase]]
 
==Reference==
<ref group="xtra">PMID:021110374</ref><references group="xtra"/><references/>
[[Category: Atcc 14581]]
[[Category: Unspecific monooxygenase]]
[[Category: Unspecific monooxygenase]]
[[Category: Bartlam, M.]]
[[Category: Bartlam, M.]]

Revision as of 07:56, 18 December 2013

Template:STRUCTURE 3m4v

Crystal structure of the A330P mutant of cytochrome P450 BM3

Template:ABSTRACT PUBMED 21110374

Function

[CPXB_BACME] Functions as a fatty acid monooxygenase. Catalyzes hydroxylation of medium and long-chain fatty acids at omega-1, omega-2 and omega-3 positions, with optimum chain lengths of 12-16 carbons (lauric, myristic, and palmitic acids). The reductase domain is required for electron transfer from NADP to cytochrome P450.

About this Structure

3m4v is a 2 chain structure with sequence from Atcc 14581. Full crystallographic information is available from OCA.

See Also

Reference

  1. Whitehouse CJ, Yang W, Yorke JA, Rowlatt BC, Strong AJ, Blanford CF, Bell SG, Bartlam M, Wong LL, Rao Z. Structural basis for the properties of two single-site proline mutants of CYP102A1 (P450BM3). Chembiochem. 2010 Dec 10;11(18):2549-56. doi: 10.1002/cbic.201000421. PMID:21110374 doi:https://dx.doi.org/10.1002/cbic.201000421

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