3i9t

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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=3i9t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3i9t OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3i9t RCSB], [http://www.ebi.ac.uk/pdbsum/3i9t 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=3i9t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3i9t OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3i9t RCSB], [http://www.ebi.ac.uk/pdbsum/3i9t PDBsum]</span></td></tr>
</table>
</table>
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== Function ==
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[[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.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]

Revision as of 18:34, 25 December 2014

Crystal structure of the rat heme oxygenase (HO-1) in complex with heme binding dithiothreitol (DTT)

3i9t, resolution 2.15Å

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