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==Rat Heme Oxygenase-1 in complex with Heme and CO with 16 hr Illumination: Laser on==
==Rat Heme Oxygenase-1 in complex with Heme and CO with 16 hr Illumination: Laser on==
<StructureSection load='4g8p' size='340' side='right' caption='[[4g8p]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='4g8p' size='340' side='right'caption='[[4g8p]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4g8p]] 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=4G8P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4G8P FirstGlance]. <br>
<table><tr><td colspan='2'>[[4g8p]] 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=4G8P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4G8P 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]], [[4g7u|4g7u]], [[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=4g8p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g8p OCA], [https://pdbe.org/4g8p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4g8p RCSB], [https://www.ebi.ac.uk/pdbsum/4g8p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4g8p 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=4g8p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g8p OCA], [http://pdbe.org/4g8p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4g8p RCSB], [http://www.ebi.ac.uk/pdbsum/4g8p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4g8p 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 4g8p" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 4g8p" 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/4g8p"