4g8u: Difference between revisions

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==Rat Heme Oxygenase-1 in complex with Heme and O2 with 13 hr illumination: Laser off==
==Rat Heme Oxygenase-1 in complex with Heme and O2 with 13 hr illumination: Laser off==
<StructureSection load='4g8u' size='340' side='right' caption='[[4g8u]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='4g8u' size='340' side='right'caption='[[4g8u]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4g8u]] 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=4G8U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4G8U FirstGlance]. <br>
<table><tr><td colspan='2'>[[4g8u]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G8U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4G8U FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene></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]], [[4g8p|4g8p]], [[4g8w|4g8w]], [[4g98|4g98]], [[4g99|4g99]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[4g7l|4g7l]], [[4g7p|4g7p]], [[4g7t|4g7t]], [[4g7u|4g7u]], [[4g8p|4g8p]], [[4g8w|4g8w]], [[4g98|4g98]], [[4g99|4g99]]</div></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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Heme_oxygenase Heme oxygenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.99.3 1.14.99.3] </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'>[https://proteopedia.org/fgij/fg.htm?mol=4g8u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g8u OCA], [https://pdbe.org/4g8u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4g8u RCSB], [https://www.ebi.ac.uk/pdbsum/4g8u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4g8u 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=4g8u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g8u OCA], [http://pdbe.org/4g8u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4g8u RCSB], [http://www.ebi.ac.uk/pdbsum/4g8u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4g8u 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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==See Also==
==See Also==
*[[Heme oxygenase|Heme oxygenase]]
*[[Heme oxygenase 3D structures|Heme oxygenase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Buffalo rat]]
[[Category: Heme oxygenase]]
[[Category: Heme oxygenase]]
[[Category: Large Structures]]
[[Category: Moffat, K]]
[[Category: Moffat, K]]
[[Category: Noguchi, M]]
[[Category: Noguchi, M]]
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