4mec
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4mec]] is a 7 chain structure. 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. 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> | ||
| - | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZNH:PROTOPORPHYRIN+IX+CONTAINING+ZN'>ZNH</scene>< | + | </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> |
| - | <tr><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='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><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://www.rcsb.org/pdb/explore.do?structureId=4mec RCSB], [http://www.ebi.ac.uk/pdbsum/4mec PDBsum]</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://www.rcsb.org/pdb/explore.do?structureId=4mec RCSB], [http://www.ebi.ac.uk/pdbsum/4mec PDBsum]</span></td></tr> |
| - | <table> | + | </table> |
| + | == 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. | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Heme oxygenase]] | [[Category: Heme oxygenase]] | ||
| - | [[Category: Sugishima, M | + | [[Category: Sugishima, M]] |
[[Category: All alpha]] | [[Category: All alpha]] | ||
[[Category: Heme binding]] | [[Category: Heme binding]] | ||
[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] | ||
[[Category: Oxygenase]] | [[Category: Oxygenase]] | ||
Revision as of 03:53, 25 December 2014
Crystal structure of RAT Heme oxygenase-1 in complex with ZN(II)-Protoporphyrin IX
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