1irm: Difference between revisions

<StructureSection load='1irm' size='340' side='right'caption='[[1irm]], [[Resolution|resolution]] 2.55&Aring;' scene=''>

<table><tr><td colspan='2'>[[1irm]] is a 3 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=1IRM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IRM FirstGlance]. <br>

</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.55&#8491;</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=1irm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1irm OCA], [https://pdbe.org/1irm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1irm RCSB], [https://www.ebi.ac.uk/pdbsum/1irm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1irm ProSAT]</span></td></tr>

[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.

[[Category: Large Structures]]

[[Category: Rattus norvegicus]]

[[Category: Fukuyama K]]

[[Category: Hayashi S]]

[[Category: Kakuta Y]]

[[Category: Noguchi M]]

[[Category: Omata Y]]

[[Category: Sakamoto H]]

[[Category: Sugishima M]]