1n6b: Difference between revisions

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 ==Microsomal Cytochrome P450 2C5/3LVdH Complex with a dimethyl derivative of sulfaphenazole==
-<StructureSection load='1n6b' size='340' side='right' caption='[[1n6b]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
+<StructureSection load='1n6b' size='340' side='right'caption='[[1n6b]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1n6b]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/European_rabbit European rabbit]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N6B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1N6B FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1n6b]] is a 1 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=1N6B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1N6B FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DMZ:4-METHYL-N-METHYL-N-(2-PHENYL-2H-PYRAZOL-3-YL)BENZENESULFONAMIDE'>DMZ</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1dt6|1dt6]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DMZ:4-METHYL-N-METHYL-N-(2-PHENYL-2H-PYRAZOL-3-YL)BENZENESULFONAMIDE'>DMZ</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CYP2C5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9986 European rabbit])</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=1n6b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n6b OCA], [https://pdbe.org/1n6b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1n6b RCSB], [https://www.ebi.ac.uk/pdbsum/1n6b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1n6b ProSAT]</span></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Unspecific_monooxygenase Unspecific monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.14.1 1.14.14.1] </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=1n6b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n6b OCA], [http://pdbe.org/1n6b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1n6b RCSB], [http://www.ebi.ac.uk/pdbsum/1n6b PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1n6b ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/CP2C5_RABIT CP2C5_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.
+[https://www.uniprot.org/uniprot/CP2C5_RABIT CP2C5_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.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 22: / Line 20: @@
 </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=1n6b ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The structure of rabbit microsomal cytochrome P450 2C5/3LVdH complexed with a substrate, 4-methyl-N-methyl-N-(2-phenyl-2H-pyrazol-3-yl)benzenesulfonamide (DMZ), was determined by X-ray crystallography to 2.3 A resolution. Substrate docking studies and electron density maps indicate that DMZ binds to the enzyme in two antiparallel orientations of the long axis of the substrate. One orientation places the principal site of hydroxylation, the 4-methyl group, 4.4 A from the heme Fe, whereas the alternate conformation positions the second, infrequent site of hydroxylation at &gt;5.9 A from the heme Fe. Comparison of this structure to that obtained previously for the enzyme indicates that the protein closes around the substrate and prevents open access of water from bulk solvent to the heme Fe. This reflects a approximately 1.5 A movement of the F and G helices relative to helix I. The present structure provides a complete model for the protein from residues 27-488 and defines two new helices F' and G'. The G' helix is likely to contribute to interactions of the enzyme with membranes. The relatively large active site, as compared to the volume occupied by the substrate, and the flexibility of the enzyme are likely to underlie the capacity of drug-metabolizing enzymes to metabolize structurally diverse substrates of different sizes.
-Structure of a substrate complex of mammalian cytochrome P450 2C5 at 2.3 A resolution: evidence for multiple substrate binding modes.,Wester MR, Johnson EF, Marques-Soares C, Dansette PM, Mansuy D, Stout CD Biochemistry. 2003 Jun 3;42(21):6370-9. PMID:12767218<ref>PMID:12767218</ref>
+==See Also==
+*[[Cytochrome P450 3D structures|Cytochrome P450 3D structures]]
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1n6b" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: European rabbit]]
+[[Category: Large Structures]]
-[[Category: Unspecific monooxygenase]]
+[[Category: Oryctolagus cuniculus]]
-[[Category: Dansette, P M]]
+[[Category: Dansette PM]]
-[[Category: Johnson, E F]]
+[[Category: Johnson EF]]
-[[Category: Mansuy, D]]
+[[Category: Mansuy D]]
-[[Category: Marques-Soares, C]]
+[[Category: Marques-Soares C]]
-[[Category: Stout, C D]]
+[[Category: Stout CD]]
-[[Category: Wester, M R]]
+[[Category: Wester MR]]
-[[Category: Cyp2c5]]
-[[Category: Dimethylsulfaphenazole complex]]
-[[Category: Estradiol 2-hydroxylase]]
-[[Category: Membrane protein]]
-[[Category: Oxidoreductase]]
-[[Category: P450]]
-[[Category: Progesterone 21-hydroxylase]]
-[[Category: Pyrene hydroxylase]]