3psx

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{{STRUCTURE_3psx| PDB=3psx | SCENE= }}
{{STRUCTURE_3psx| PDB=3psx | SCENE= }}
===Crystal structure of the KT2 mutant of cytochrome P450 BM3===
===Crystal structure of the KT2 mutant of cytochrome P450 BM3===
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{{ABSTRACT_PUBMED_21603690}}
==Function==
==Function==
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==About this Structure==
==About this Structure==
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[[3psx]] 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=3PSX OCA].
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[[3psx]] 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=3PSX OCA].
==See Also==
==See Also==
*[[Cytochrome P450|Cytochrome P450]]
*[[Cytochrome P450|Cytochrome P450]]
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[[Category: Bacillus megaterium]]
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*[[NADPH-Cytochrome P450 Reductase|NADPH-Cytochrome P450 Reductase]]
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==Reference==
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<ref group="xtra">PMID:021603690</ref><references group="xtra"/><references/>
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[[Category: Atcc 14581]]
[[Category: Unspecific monooxygenase]]
[[Category: Unspecific monooxygenase]]
[[Category: Bartlam, M.]]
[[Category: Bartlam, M.]]

Revision as of 07:40, 18 December 2013

Template:STRUCTURE 3psx

Contents

Crystal structure of the KT2 mutant of cytochrome P450 BM3

Template:ABSTRACT PUBMED 21603690

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

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

See Also

Reference

  • Whitehouse CJ, Yang W, Yorke JA, Tufton HG, Ogilvie LC, Bell SG, Zhou W, Bartlam M, Rao Z, Wong LL. Structure, electronic properties and catalytic behaviour of an activity-enhancing CYP102A1 (P450(BM3)) variant. Dalton Trans. 2011 Oct 28;40(40):10383-96. doi: 10.1039/c1dt10098j. Epub 2011 May, 20. PMID:21603690 doi:http://dx.doi.org/10.1039/c1dt10098j

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