4g8p: Difference between revisions
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<StructureSection load='4g8p' size='340' side='right'caption='[[4g8p]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='4g8p' size='340' side='right'caption='[[4g8p]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4g8p]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G8P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4G8P FirstGlance]. <br> | <table><tr><td colspan='2'>[[4g8p]] 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=4G8P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4G8P 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]] 1.9Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CMO:CARBON+MONOXIDE'>CMO</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</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=4g8p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g8p OCA], [https://pdbe.org/4g8p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4g8p RCSB], [https://www.ebi.ac.uk/pdbsum/4g8p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4g8p 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=4g8p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g8p OCA], [https://pdbe.org/4g8p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4g8p RCSB], [https://www.ebi.ac.uk/pdbsum/4g8p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4g8p 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]] | ||