2j4s: 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='2j4s' size='340' side='right' caption='[[2j4s]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='2j4s' size='340' side='right' caption='[[2j4s]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1bu7|1bu7]], [[1bvy|1bvy]], [[1fag|1fag]], [[1fah|1fah]], [[1jme|1jme]], [[1jpz|1jpz]], [[1p0v|1p0v]], [[1p0w|1p0w]], [[1p0x|1p0x]], [[1smi|1smi]], [[1smj|1smj]], [[1yqo|1yqo]], [[1yqp|1yqp]], [[2bmh|2bmh]], [[2hpd|2hpd]], [[2j1m|2j1m]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1bu7|1bu7]], [[1bvy|1bvy]], [[1fag|1fag]], [[1fah|1fah]], [[1jme|1jme]], [[1jpz|1jpz]], [[1p0v|1p0v]], [[1p0w|1p0w]], [[1p0x|1p0x]], [[1smi|1smi]], [[1smj|1smj]], [[1yqo|1yqo]], [[1yqp|1yqp]], [[2bmh|2bmh]], [[2hpd|2hpd]], [[2j1m|2j1m]]</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Unspecific_monooxygenase Unspecific monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.14.1 1.14.14.1] </span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Unspecific_monooxygenase Unspecific monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.14.1 1.14.14.1] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2j4s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j4s OCA], [http://pdbe.org/2j4s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2j4s RCSB], [http://www.ebi.ac.uk/pdbsum/2j4s PDBsum]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2j4s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j4s OCA], [http://pdbe.org/2j4s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2j4s RCSB], [http://www.ebi.ac.uk/pdbsum/2j4s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2j4s ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/j4/2j4s_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/j4/2j4s_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
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==See Also==
==See Also==
*[[Cytochrome P450|Cytochrome P450]]
*[[Cytochrome P450|Cytochrome P450]]
*[[Flavocytochrome|Flavocytochrome]]
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Revision as of 10:12, 11 July 2018

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

Structural highlights

2j4s 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

2j4s, resolution 2.10Å

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