5b2x
From Proteopedia
(Difference between revisions)
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==Crystal Structure of P450BM3 mutant with N-perfluoroheptanoyl-L-tryptophan== | ==Crystal Structure of P450BM3 mutant with N-perfluoroheptanoyl-L-tryptophan== | ||
| - | <StructureSection load='5b2x' size='340' side='right' caption='[[5b2x]], [[Resolution|resolution]] 1.90Å' scene=''> | + | <StructureSection load='5b2x' size='340' side='right'caption='[[5b2x]], [[Resolution|resolution]] 1.90Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5b2x]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5B2X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5B2X FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5b2x]] 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=5B2X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5B2X 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=W0T:(2~{S})-3-(1~{H}-INDOL-3-YL)-2-[2,2,3,3,4,4,5,5,6,6,7,7,7-TRIDECAKIS(FLUORANYL)HEPTANOYLAMINO]PROPANOIC+ACID'>W0T</scene></td></tr> | </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=W0T:(2~{S})-3-(1~{H}-INDOL-3-YL)-2-[2,2,3,3,4,4,5,5,6,6,7,7,7-TRIDECAKIS(FLUORANYL)HEPTANOYLAMINO]PROPANOIC+ACID'>W0T</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3wsp|3wsp]], [[5b2u|5b2u]], [[5b2v|5b2v]], [[5b2w|5b2w]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3wsp|3wsp]], [[5b2u|5b2u]], [[5b2v|5b2v]], [[5b2w|5b2w]]</td></tr> | ||
| + | <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> | ||
<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=5b2x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b2x OCA], [http://pdbe.org/5b2x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5b2x RCSB], [http://www.ebi.ac.uk/pdbsum/5b2x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5b2x ProSAT]</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=5b2x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b2x OCA], [http://pdbe.org/5b2x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5b2x RCSB], [http://www.ebi.ac.uk/pdbsum/5b2x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5b2x ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[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. | [[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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| + | ==See Also== | ||
| + | *[[Cytochrome P450 3D structures|Cytochrome P450 3D structures]] | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Atcc 14581]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Cong, Z]] | [[Category: Cong, Z]] | ||
[[Category: Kasai, C]] | [[Category: Kasai, C]] | ||
Revision as of 10:02, 26 February 2020
Crystal Structure of P450BM3 mutant with N-perfluoroheptanoyl-L-tryptophan
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