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==Rat Heme Oxygenase-1 in complex with Heme and CO with 16 hr Illumination: Laser off==
==Rat Heme Oxygenase-1 in complex with Heme and CO with 16 hr Illumination: Laser off==
<StructureSection load='4g7u' size='340' side='right' caption='[[4g7u]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='4g7u' size='340' side='right'caption='[[4g7u]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4g7u]] 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=4G7U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4G7U FirstGlance]. <br>
<table><tr><td colspan='2'>[[4g7u]] 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=4G7U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4G7U 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=FMT:FORMIC+ACID'>FMT</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]] 1.9&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4g7l|4g7l]], [[4g7p|4g7p]], [[4g7t|4g7t]], [[4g8p|4g8p]], [[4g8u|4g8u]], [[4g8w|4g8w]], [[4g98|4g98]], [[4g99|4g99]]</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=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Hmox1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</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=4g7u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g7u OCA], [https://pdbe.org/4g7u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4g7u RCSB], [https://www.ebi.ac.uk/pdbsum/4g7u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4g7u 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/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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4g7u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g7u OCA], [http://pdbe.org/4g7u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4g7u RCSB], [http://www.ebi.ac.uk/pdbsum/4g7u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4g7u 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.
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 4g7u" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 4g7u" 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: Moffat, K]]
[[Category: Moffat K]]
[[Category: Noguchi, M]]
[[Category: Noguchi M]]
[[Category: Sugishima, M]]
[[Category: Sugishima M]]
[[Category: All alpha protein]]
[[Category: Oxidoreductase]]
[[Category: Oxygenase]]
Retrieved from "https://proteopedia.org/4g7u"