5uca: Difference between revisions
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==Crystal structure of human Heme Oxygenase-2 in complex with Laurate== | ==Crystal structure of human Heme Oxygenase-2 in complex with Laurate== | ||
<StructureSection load='5uca' size='340' side='right' caption='[[5uca]], [[Resolution|resolution]] 2.12Å' scene=''> | <StructureSection load='5uca' size='340' side='right'caption='[[5uca]], [[Resolution|resolution]] 2.12Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5uca]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UCA OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[5uca]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UCA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5UCA 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]] 2.117Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DAO:LAURIC+ACID'>DAO</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=5uca FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uca OCA], [https://pdbe.org/5uca PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5uca RCSB], [https://www.ebi.ac.uk/pdbsum/5uca PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5uca ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/HMOX2_HUMAN HMOX2_HUMAN] 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. Heme oxygenase 2 could be implicated in the production of carbon monoxide in brain where it could act as a neurotransmitter. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 5uca" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5uca" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Heme oxygenase 3D structures|Heme oxygenase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Luo S]] | ||
[[Category: | [[Category: Tong L]] | ||