5uec: Difference between revisions
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<StructureSection load='5uec' size='340' side='right' caption='[[5uec]], [[Resolution|resolution]] 2.27Å' scene=''> | <StructureSection load='5uec' size='340' side='right' caption='[[5uec]], [[Resolution|resolution]] 2.27Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5uec]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UEC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5UEC FirstGlance]. <br> | <table><tr><td colspan='2'>[[5uec]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UEC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5UEC FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=85D:(1S,5R)-2-(BROMOMETHYL)-6,6-DIMETHYLBICYCLO[3.1.1]HEPT-2-ENE'>85D</scene>, <scene name='pdbligand=CM5:5-CYCLOHEXYL-1-PENTYL-BETA-D-MALTOSIDE'>CM5</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=85D:(1S,5R)-2-(BROMOMETHYL)-6,6-DIMETHYLBICYCLO[3.1.1]HEPT-2-ENE'>85D</scene>, <scene name='pdbligand=CM5:5-CYCLOHEXYL-1-PENTYL-BETA-D-MALTOSIDE'>CM5</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5uda|5uda]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5uda|5uda]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CYP2B6 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=5uec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uec OCA], [http://pdbe.org/5uec PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5uec RCSB], [http://www.ebi.ac.uk/pdbsum/5uec PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5uec 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=5uec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uec OCA], [http://pdbe.org/5uec PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5uec RCSB], [http://www.ebi.ac.uk/pdbsum/5uec PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5uec ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Human]] | |||
[[Category: Halpert, J R]] | [[Category: Halpert, J R]] | ||
[[Category: Shah, M B]] | [[Category: Shah, M B]] | ||
[[Category: Cytochrome p450 2b6]] | [[Category: Cytochrome p450 2b6]] | ||
[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] | ||
Revision as of 17:33, 6 November 2017
Crystal Structure of CYP2B6 (Y226H/K262R) in complex with myrtenyl bromide.Crystal Structure of CYP2B6 (Y226H/K262R) in complex with myrtenyl bromide.
Structural highlights
Function[CP2B6_HUMAN] Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. Acts as a 1,4-cineole 2-exo-monooxygenase.[1] Publication Abstract from PubMedNumerous cytochrome P450 (CYP) 2B6 substrates including drugs and environmental chemicals are halogenated. To assess the role of halogen-pi bonds in substrate selectivity and orientation in the active site, structures of four CYP2B6 monoterpenoid complexes were solved by X-ray crystallography. Bornyl bromide exhibited dual orientations in the active site with the predominant orientation revealing a bromine-pi bond with the Phe108 side chain. Bornane demonstrated two orientations with equal occupancy; in both, the C2 atom that bears the bromine in bornyl bromide was displaced by more than 2.5 A compared with the latter complex. The bromine in myrtenyl bromide pi-bonded with Phe297 in CYP2B6, whereas the two major orientations in the active site mutant I114V exhibited bromine-pi interactions with two additional residues, Phe108 and Phe115. Analysis of existing structures suggests that halogen-pi interactions may be unique to the CYP2B enzymes within CYP family 2 but are also important for CYP3A enzymes. Halogen-pi Interactions in the Cytochrome P450 Active Site: Structural Insights into Human CYP2B6 Substrate Selectivity.,Shah MB, Liu J, Zhang Q, Stout CD, Halpert JR ACS Chem Biol. 2017 Apr 6. doi: 10.1021/acschembio.7b00056. PMID:28368100[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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