4g8p: Difference between revisions

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<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://www.rcsb.org/pdb/explore.do?structureId=4g8p RCSB], [http://www.ebi.ac.uk/pdbsum/4g8p PDBsum]</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://www.rcsb.org/pdb/explore.do?structureId=4g8p RCSB], [http://www.ebi.ac.uk/pdbsum/4g8p PDBsum]</span></td></tr>
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</table>
== 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.
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==