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==Structure of heme oxygenase-2 containing residues 1-288 lacking the membrane spanning region== | ==Structure of heme oxygenase-2 containing residues 1-288 lacking the membrane spanning region== | ||
<StructureSection load='4wmh' size='340' side='right' caption='[[4wmh]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='4wmh' size='340' side='right'caption='[[4wmh]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4wmh]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WMH OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[4wmh]] is a 1 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=4WMH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WMH 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]] 2.5Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</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=4wmh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wmh OCA], [https://pdbe.org/4wmh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wmh RCSB], [https://www.ebi.ac.uk/pdbsum/4wmh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wmh ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== 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. | |||
==See Also== | |||
*[[Heme oxygenase 3D structures|Heme oxygenase 3D structures]] | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Bianchetti CM]] | ||
[[Category: Li | [[Category: Li Y]] | ||
[[Category: Phillips | [[Category: Phillips Jr GN]] | ||
[[Category: Ragsdale | [[Category: Ragsdale SW]] | ||
Latest revision as of 10:33, 27 September 2023
Structure of heme oxygenase-2 containing residues 1-288 lacking the membrane spanning regionStructure of heme oxygenase-2 containing residues 1-288 lacking the membrane spanning region
Structural highlights
FunctionHMOX2_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. See Also |
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