5b2v

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<StructureSection load='5b2v' size='340' side='right'caption='[[5b2v]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='5b2v' size='340' side='right'caption='[[5b2v]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5b2v]] 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=5B2V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5B2V FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5b2v]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Priestia_megaterium Priestia megaterium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5B2V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5B2V FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=W06:(2~{S})-3-(1~{H}-INDOL-3-YL)-2-[2,2,3,3,4,4,5,5,6,6,6-UNDECAKIS(FLUORANYL)HEXANOYLAMINO]PROPANOIC+ACID'>W06</scene></td></tr>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=W06:(2~{S})-3-(1~{H}-INDOL-3-YL)-2-[2,2,3,3,4,4,5,5,6,6,6-UNDECAKIS(FLUORANYL)HEXANOYLAMINO]PROPANOIC+ACID'>W06</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3wsp|3wsp]], [[5b2u|5b2u]], [[5b2w|5b2w]], [[5b2x|5b2x]]</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5b2v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b2v OCA], [https://pdbe.org/5b2v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5b2v RCSB], [https://www.ebi.ac.uk/pdbsum/5b2v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5b2v ProSAT]</span></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cyp102A1, cyp102 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1404 ATCC 14581])</td></tr>
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<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=5b2v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b2v OCA], [http://pdbe.org/5b2v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5b2v RCSB], [http://www.ebi.ac.uk/pdbsum/5b2v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5b2v ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://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.
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[https://www.uniprot.org/uniprot/CPXB_PRIM2 CPXB_PRIM2] Functions as a fatty acid monooxygenase (PubMed:3106359, PubMed:1727637, PubMed:16566047, PubMed:7578081, PubMed:11695892, PubMed:14653735, PubMed:16403573, PubMed:18004886, PubMed:17077084, PubMed:17868686, PubMed:18298086, PubMed:18619466, PubMed:18721129, PubMed:19492389, PubMed:20180779, PubMed:21110374, PubMed:21875028). Catalyzes hydroxylation of fatty acids at omega-1, omega-2 and omega-3 positions (PubMed:1727637, PubMed:21875028). Shows activity toward medium and long-chain fatty acids, with optimum chain lengths of 12, 14 and 16 carbons (lauric, myristic, and palmitic acids). Able to metabolize some of these primary metabolites to secondary and tertiary products (PubMed:1727637). Marginal activity towards short chain lengths of 8-10 carbons (PubMed:1727637, PubMed:18619466). Hydroxylates highly branched fatty acids, which play an essential role in membrane fluidity regulation (PubMed:16566047). Also displays a NADPH-dependent reductase activity in the C-terminal domain, which allows electron transfer from NADPH to the heme iron of the cytochrome P450 N-terminal domain (PubMed:3106359, PubMed:1727637, PubMed:16566047, PubMed:7578081, PubMed:11695892, PubMed:14653735, PubMed:16403573, PubMed:18004886, PubMed:17077084, PubMed:17868686, PubMed:18298086, PubMed:18619466, PubMed:18721129, PubMed:19492389, PubMed:20180779, PubMed:21110374, PubMed:21875028). Involved in inactivation of quorum sensing signals of other competing bacteria by oxidazing efficiently acyl homoserine lactones (AHLs), molecules involved in quorum sensing signaling pathways, and their lactonolysis products acyl homoserines (AHs) (PubMed:18020460).<ref>PMID:11695892</ref> <ref>PMID:14653735</ref> <ref>PMID:16403573</ref> <ref>PMID:16566047</ref> <ref>PMID:17077084</ref> <ref>PMID:1727637</ref> <ref>PMID:17868686</ref> <ref>PMID:18004886</ref> <ref>PMID:18020460</ref> <ref>PMID:18298086</ref> <ref>PMID:18619466</ref> <ref>PMID:18721129</ref> <ref>PMID:19492389</ref> <ref>PMID:20180779</ref> <ref>PMID:21110374</ref> <ref>PMID:21875028</ref> <ref>PMID:3106359</ref> <ref>PMID:7578081</ref>
==See Also==
==See Also==
*[[Cytochrome P450 3D structures|Cytochrome P450 3D structures]]
*[[Cytochrome P450 3D structures|Cytochrome P450 3D structures]]
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Atcc 14581]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Cong, Z]]
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[[Category: Priestia megaterium]]
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[[Category: Kasai, C]]
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[[Category: Cong Z]]
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[[Category: Shiro, Y]]
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[[Category: Kasai C]]
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[[Category: Shoji, O]]
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[[Category: Shiro Y]]
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[[Category: Sugimoto, H]]
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[[Category: Shoji O]]
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[[Category: Watanabe, Y]]
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[[Category: Sugimoto H]]
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[[Category: Cytochrome p450]]
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[[Category: Watanabe Y]]
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[[Category: Oxidoreductase]]
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Revision as of 06:37, 31 May 2023

Crystal Structure of P450BM3 with N-perfluorohexanoyl-L-tryptophan

PDB ID 5b2v

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