2j1m: Difference between revisions

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==P450 BM3 Heme domain in complex with DMSO==
==P450 BM3 Heme domain in complex with DMSO==
<StructureSection load='2j1m' size='340' side='right' caption='[[2j1m]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
<StructureSection load='2j1m' size='340' side='right'caption='[[2j1m]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2j1m]] 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=2J1M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2J1M FirstGlance]. <br>
<table><tr><td colspan='2'>[[2j1m]] 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=2J1M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2J1M FirstGlance]. <br>
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==See Also==
==See Also==
*[[Cytochrome P450|Cytochrome P450]]
*[[Cytochrome P450 3D structures|Cytochrome P450 3D structures]]
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 14581]]
[[Category: Atcc 14581]]
[[Category: Large Structures]]
[[Category: Unspecific monooxygenase]]
[[Category: Unspecific monooxygenase]]
[[Category: Kuper, J]]
[[Category: Kuper, J]]

Revision as of 10:21, 24 July 2019

P450 BM3 Heme domain in complex with DMSOP450 BM3 Heme domain in complex with DMSO

Structural highlights

2j1m is a 2 chain structure with sequence from Atcc 14581. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, ,
Activity:Unspecific monooxygenase, with EC number 1.14.14.1
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

2j1m, resolution 1.70Å

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