2j1m: Difference between revisions
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<StructureSection load='2j1m' size='340' side='right'caption='[[2j1m]], [[Resolution|resolution]] 1.70Å' scene=''> | <StructureSection load='2j1m' size='340' side='right'caption='[[2j1m]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2j1m]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2j1m]] is a 2 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=2J1M FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[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]]</div></td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Unspecific_monooxygenase Unspecific monooxygenase], with EC number [https://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'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2j1m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j1m OCA], [https://pdbe.org/2j1m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2j1m RCSB], [https://www.ebi.ac.uk/pdbsum/2j1m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2j1m ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/CPXB_BACME 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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 13:06, 12 May 2021
P450 BM3 Heme domain in complex with DMSOP450 BM3 Heme domain in complex with DMSO
Structural highlights
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 |
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