2zvu: Difference between revisions
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<StructureSection load='2zvu' size='340' side='right'caption='[[2zvu]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='2zvu' size='340' side='right'caption='[[2zvu]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2zvu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2zvu]] 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=2ZVU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZVU 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]] 2.2Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=VEA:5-OXA-PROTOPORPHYRIN+IX+CONTAINING+FE'>VEA</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=2zvu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zvu OCA], [https://pdbe.org/2zvu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zvu RCSB], [https://www.ebi.ac.uk/pdbsum/2zvu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zvu 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=2zvu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zvu OCA], [https://pdbe.org/2zvu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zvu RCSB], [https://www.ebi.ac.uk/pdbsum/2zvu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zvu 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: Noguchi | [[Category: Fukuyama K]] | ||
[[Category: Sato | [[Category: Noguchi M]] | ||
[[Category: Sugishima | [[Category: Sato H]] | ||
[[Category: Sugishima M]] | |||