1ix3: Difference between revisions
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<StructureSection load='1ix3' size='340' side='right'caption='[[1ix3]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='1ix3' size='340' side='right'caption='[[1ix3]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1ix3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1ix3]] 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=1IX3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IX3 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CYN:CYANIDE+ION'>CYN</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></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=1ix3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ix3 OCA], [https://pdbe.org/1ix3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ix3 RCSB], [https://www.ebi.ac.uk/pdbsum/1ix3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ix3 ProSAT]</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=1ix3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ix3 OCA], [https://pdbe.org/1ix3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ix3 RCSB], [https://www.ebi.ac.uk/pdbsum/1ix3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ix3 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[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. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Fukuyama | [[Category: Rattus norvegicus]] | ||
[[Category: Hayashi | [[Category: Fukuyama K]] | ||
[[Category: Noguchi | [[Category: Hayashi S]] | ||
[[Category: Omata | [[Category: Noguchi M]] | ||
[[Category: Sakamoto | [[Category: Omata Y]] | ||
[[Category: Sugishima | [[Category: Sakamoto H]] | ||
[[Category: Sugishima M]] | |||