3g5n

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{{Seed}}
 
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[[Image:3g5n.png|left|200px]]
 
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==Triple ligand occupancy crystal structure of cytochrome P450 2B4 in complex with the inhibitor 1-biphenyl-4-methyl-1H-imidazole==
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The line below this paragraph, containing "STRUCTURE_3g5n", creates the "Structure Box" on the page.
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<StructureSection load='3g5n' size='340' side='right'caption='[[3g5n]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3g5n]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3G5N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3G5N FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CM5:5-CYCLOHEXYL-1-PENTYL-BETA-D-MALTOSIDE'>CM5</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=PB2:1-(BIPHENYL-4-YLMETHYL)-1H-IMIDAZOLE'>PB2</scene></td></tr>
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{{STRUCTURE_3g5n| PDB=3g5n | SCENE= }}
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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=3g5n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3g5n OCA], [https://pdbe.org/3g5n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3g5n RCSB], [https://www.ebi.ac.uk/pdbsum/3g5n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3g5n ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CP2B4_RABIT CP2B4_RABIT] 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. In the epoxidation of arachidonic acid it has a unique preference for the 5,6-olefin.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g5/3g5n_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3g5n ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Two different ligand occupancy structures of cytochrome P450 2B4 (CYP2B4) in complex with 1-biphenyl-4-methyl-1H-imidazole (1-PBI) have been solved by x-ray crystallography. 1-PBI belongs to a series of tight binding, imidazole-based CYP2B4 inhibitors. 1-PBI binding to CYP2B4 yields a type II spectrum with a Ks value of 0.23 microM and inhibits enzyme activity with an IC50 value of 0.035 microM. Previous CYP2B4 structures have shown a large degree of structural movement in response to ligand size. With two phenyl rings, 1-PBI is larger than 1-(4-chlorophenyl)imidazole (1-CPI) and 4-(4-chlorophenyl)imidazole (4-CPI) but smaller than bifonazole, which is branched and contains three phenyl rings. The CYP2B4:1-PBI complex is a structural intermediate to the closed CPI and the open bifonazole structures. The B/C loop reorganizes itself to include two short partial helices while closing one side of the active site. The F-G helix cassette pivots over the I-helix in direct response to the size of the ligand in the active site. A cluster of Phe residues at the fulcrum of this pivot point allows for dramatic repositioning of the cassette with only a relatively small amount of secondary structure rearrangement. Comparisons of ligand bound CYP2B4 structures reveal trends in plastic region mobility that could allow for predictions of their position in future structures based on ligand shape and size.
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===Triple ligand occupancy crystal structure of cytochrome P450 2B4 in complex with the inhibitor 1-biphenyl-4-methyl-1H-imidazole===
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Crystal structures of cytochrome P450 2B4 in complex with the inhibitor 1-biphenyl-4-methyl-1Himidazole: ligand induced structural response through -helical repositioning.,Gay SC, Sun L, Maekawa K, Halpert JR, Stout CD Biochemistry. 2009 Apr 27. PMID:19397311<ref>PMID:19397311</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3g5n" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_19397311}}, adds the Publication Abstract to the page
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*[[Cytochrome P450 3D structures|Cytochrome P450 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 19397311 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_19397311}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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3G5N is a 4 chains structure of sequences from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3G5N OCA].
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==Reference==
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<ref group="xtra">PMID:19397311</ref><references group="xtra"/>
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[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
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[[Category: Unspecific monooxygenase]]
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[[Category: Gay SC]]
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[[Category: Gay, S C.]]
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[[Category: Halpert JR]]
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[[Category: Halpert, J R.]]
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[[Category: Maekawa K]]
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[[Category: Maekawa, K.]]
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[[Category: Stout CD]]
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[[Category: Stout, C D.]]
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[[Category: Sun L]]
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[[Category: Sun, L.]]
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[[Category: Cyp 2b4]]
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[[Category: Cyp lm2]]
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[[Category: Cytochrome p450 2b4]]
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[[Category: Endoplasmic reticulum]]
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[[Category: Heme]]
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[[Category: Iron]]
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[[Category: Membrane]]
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[[Category: Membrane protein]]
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[[Category: Metal-binding]]
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[[Category: Microsome]]
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[[Category: Monooxygenase]]
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[[Category: Oxidoreductase]]
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[[Category: P450]]
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[[Category: Phosphoprotein]]
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[[Category: Polymorphism]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 10 14:30:11 2009''
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Current revision

Triple ligand occupancy crystal structure of cytochrome P450 2B4 in complex with the inhibitor 1-biphenyl-4-methyl-1H-imidazole

PDB ID 3g5n

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