3i9u: Difference between revisions
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<StructureSection load='3i9u' size='340' side='right'caption='[[3i9u]], [[Resolution|resolution]] 2.25Å' scene=''> | <StructureSection load='3i9u' size='340' side='right'caption='[[3i9u]], [[Resolution|resolution]] 2.25Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3i9u]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3i9u]] 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=3I9U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3I9U 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]] 2.25Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DTU:(2R,3S)-1,4-DIMERCAPTOBUTANE-2,3-DIOL'>DTU</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr> | |||
<tr id=' | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3i9u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3i9u OCA], [https://pdbe.org/3i9u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3i9u RCSB], [https://www.ebi.ac.uk/pdbsum/3i9u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3i9u 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=3i9u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3i9u OCA], [https://pdbe.org/3i9u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3i9u RCSB], [https://www.ebi.ac.uk/pdbsum/3i9u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3i9u 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: Ikeda-Saito | [[Category: Rattus norvegicus]] | ||
[[Category: Matsui | [[Category: Ikeda-Saito M]] | ||
[[Category: Unno | [[Category: Matsui T]] | ||
[[Category: Unno M]] | |||