1ix4: Difference between revisions

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==Crystal Structure of Rat Heme Oxygenase-1 in complex with Heme bound to Carbon Monoxide==
==Crystal Structure of Rat Heme Oxygenase-1 in complex with Heme bound to Carbon Monoxide==
<StructureSection load='1ix4' size='340' side='right' caption='[[1ix4]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='1ix4' size='340' side='right'caption='[[1ix4]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1ix4]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IX4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IX4 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1ix4]] 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=1IX4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IX4 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CMO:CARBON+MONOXIDE'>CMO</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</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]] 1.8&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1dve|1dve]], [[1ivj|1ivj]], [[1qq8|1qq8]], [[1j77|1j77]], [[1ix3|1ix3]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CMO:CARBON+MONOXIDE'>CMO</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
<tr id='activity'><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=1ix4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ix4 OCA], [https://pdbe.org/1ix4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ix4 RCSB], [https://www.ebi.ac.uk/pdbsum/1ix4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ix4 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=1ix4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ix4 OCA], [http://pdbe.org/1ix4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ix4 RCSB], [http://www.ebi.ac.uk/pdbsum/1ix4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ix4 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://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.  
[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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ix/1ix4_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ix/1ix4_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </jmolCheckbox>
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</div>
</div>
<div class="pdbe-citations 1ix4" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 1ix4" style="background-color:#fffaf0;"></div>
==See Also==
*[[Heme oxygenase 3D structures|Heme oxygenase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Buffalo rat]]
[[Category: Large Structures]]
[[Category: Heme oxygenase]]
[[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: Hemeprotein]]
[[Category: Inhibitor complex]]
[[Category: Oxidoreductase]]
Retrieved from "https://proteopedia.org/1ix4"