View source for 5ufg


==Crystal Structure of CYP2B6 (Y226H/K262R/I114V) in complex with myrtenyl bromide==
<StructureSection load='5ufg' size='340' side='right'caption='[[5ufg]], [[Resolution|resolution]] 1.76&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5ufg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UFG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5UFG FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.76&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5ufg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ufg OCA], [https://pdbe.org/5ufg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ufg RCSB], [https://www.ebi.ac.uk/pdbsum/5ufg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ufg ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CP2B6_HUMAN 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.<ref>PMID:11695850</ref> 
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== Publication Abstract from PubMed ==
Numerous 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<ref>PMID:28368100</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 5ufg" style="background-color:#fffaf0;"></div>

==See Also==
*[[Cytochrome P450 3D structures|Cytochrome P450 3D structures]]
== References ==
<references/>
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Halpert JR]]
[[Category: Shah MB]]