5b2x
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal Structure of P450BM3 mutant with N-perfluoroheptanoyl-L-tryptophan== | |
| - | + | <StructureSection load='5b2x' size='340' side='right' caption='[[5b2x]], [[Resolution|resolution]] 1.90Å' scene=''> | |
| - | + | == 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> | |
| - | + | </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> | |
| - | [[Category: | + | <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='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> | ||
| + | == 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. | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Cong, Z]] | ||
| + | [[Category: Kasai, C]] | ||
[[Category: Shiro, Y]] | [[Category: Shiro, Y]] | ||
| + | [[Category: Shoji, O]] | ||
[[Category: Sugimoto, H]] | [[Category: Sugimoto, H]] | ||
| - | [[Category: Cong, Z]] | ||
| - | [[Category: Shoji, O]] | ||
| - | [[Category: Kasai, C]] | ||
[[Category: Watanabe, Y]] | [[Category: Watanabe, Y]] | ||
| + | [[Category: Cytochrome p450]] | ||
| + | [[Category: Oxidoreductase]] | ||
Revision as of 09:20, 10 March 2017
Crystal Structure of P450BM3 mutant with N-perfluoroheptanoyl-L-tryptophan
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Categories: Cong, Z | Kasai, C | Shiro, Y | Shoji, O | Sugimoto, H | Watanabe, Y | Cytochrome p450 | Oxidoreductase
