1ix3: Difference between revisions

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 ==Crystal Structure of Rat Heme Oxygenase-1 in complex with Heme bound to Cyanide==
-<StructureSection load='1ix3' size='340' side='right' caption='[[1ix3]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+<StructureSection load='1ix3' size='340' side='right'caption='[[1ix3]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1ix3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IX3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IX3 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1ix3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IX3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IX3 FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CYN:CYANIDE+ION'>CYN</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene><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]] 2&#8491;</td></tr>
-<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1dve|1dve]], [[1ivj|1ivj]], [[1qq8|1qq8]], [[1j77|1j77]], [[1ix4|1ix4]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CYN:CYANIDE+ION'>CYN</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
-<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Heme_oxygenase Heme oxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.99.3 1.14.99.3] </span></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=1ix3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ix3 OCA], [https://pdbe.org/1ix3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ix3 RCSB], [https://www.ebi.ac.uk/pdbsum/1ix3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ix3 ProSAT]</span></td></tr>
-<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ix3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ix3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ix3 RCSB], [http://www.ebi.ac.uk/pdbsum/1ix3 PDBsum]</span></td></tr>
+</table>
-<table>
+== Function ==
+[https://www.uniprot.org/uniprot/HMOX1_RAT HMOX1_RAT] Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
 Check<jmol>
    <jmolCheckbox>
-     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ix/1ix3_consurf.spt"</scriptWhenChecked>
+     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ix/1ix3_consurf.spt"</scriptWhenChecked>
      <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
      <text>to colour the structure by Evolutionary Conservation</text>
    </jmolCheckbox>
-</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/chain_selection.php?pdb_ID=2ata ConSurf].
+</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=1ix3 ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 26: / Line 28: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1ix3" style="background-color:#fffaf0;"></div>
 ==See Also==
-*[[Heme oxygenase|Heme oxygenase]]
+*[[Heme oxygenase 3D structures|Heme oxygenase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Heme oxygenase]]
+[[Category: Large Structures]]
 [[Category: Rattus norvegicus]]
-[[Category: Fukuyama, K.]]
+[[Category: Fukuyama K]]
-[[Category: Hayashi, S.]]
+[[Category: Hayashi S]]
-[[Category: Noguchi, M.]]
+[[Category: Noguchi M]]
-[[Category: Omata, Y.]]
+[[Category: Omata Y]]
-[[Category: Sakamoto, H.]]
+[[Category: Sakamoto H]]
-[[Category: Sugishima, M.]]
+[[Category: Sugishima M]]
-[[Category: Co-analog complex]]
-[[Category: Hemeprotein]]
-[[Category: Inhibitor complex]]
-[[Category: Oxidoreductase]]