4mec: Difference between revisions

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<StructureSection load='4mec' size='340' side='right'caption='[[4mec]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
<StructureSection load='4mec' size='340' side='right'caption='[[4mec]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4mec]] is a 7 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MEC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4MEC FirstGlance]. <br>
<table><tr><td colspan='2'>[[4mec]] is a 7 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=4MEC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MEC FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZNH:PROTOPORPHYRIN+IX+CONTAINING+ZN'>ZNH</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.2&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Hmox1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</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=4mec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mec OCA], [https://pdbe.org/4mec PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4mec RCSB], [https://www.ebi.ac.uk/pdbsum/4mec PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4mec ProSAT]</span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Heme_oxygenase Heme oxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.99.3 1.14.99.3] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4mec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mec OCA], [http://pdbe.org/4mec PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4mec RCSB], [http://www.ebi.ac.uk/pdbsum/4mec PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4mec ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://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.  
[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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==See Also==
==See Also==
*[[Heme oxygenase|Heme oxygenase]]
*[[Heme oxygenase 3D structures|Heme oxygenase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Buffalo rat]]
[[Category: Heme oxygenase]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Sugishima, M]]
[[Category: Rattus norvegicus]]
[[Category: All alpha]]
[[Category: Sugishima M]]
[[Category: Heme binding]]
[[Category: Oxidoreductase]]
[[Category: Oxygenase]]
Retrieved from "https://proteopedia.org/4mec"