4g7l: Difference between revisions
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<StructureSection load='4g7l' size='340' side='right'caption='[[4g7l]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='4g7l' size='340' side='right'caption='[[4g7l]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4g7l]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G7L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4G7L FirstGlance]. <br> | <table><tr><td colspan='2'>[[4g7l]] 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=4G7L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4G7L 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]] 1.8Å</td></tr> | ||
<tr id=' | <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=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</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=4g7l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g7l OCA], [https://pdbe.org/4g7l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4g7l RCSB], [https://www.ebi.ac.uk/pdbsum/4g7l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4g7l 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=4g7l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g7l OCA], [https://pdbe.org/4g7l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4g7l RCSB], [https://www.ebi.ac.uk/pdbsum/4g7l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4g7l 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. | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Rattus norvegicus]] | ||
[[Category: | [[Category: Moffat K]] | ||
[[Category: | [[Category: Noguchi M]] | ||
[[Category: | [[Category: Sugishima M]] | ||