4wd4
From Proteopedia
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| - | ''' | + | ==Crystal structure of human HO1 H25R== |
| - | + | <StructureSection load='4wd4' size='340' side='right' caption='[[4wd4]], [[Resolution|resolution]] 2.95Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[4wd4]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WD4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WD4 FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></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=4wd4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wd4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4wd4 RCSB], [http://www.ebi.ac.uk/pdbsum/4wd4 PDBsum]</span></td></tr> | |
| - | [[ | + | </table> |
| - | [[Category: | + | == Disease == |
| - | [[Category: Caaveiro, J | + | [[http://www.uniprot.org/uniprot/HMOX1_HUMAN HMOX1_HUMAN]] Defects in HMOX1 are the cause of heme oxygenase 1 deficiency (HMOX1D) [MIM:[http://omim.org/entry/614034 614034]]. A disease characterized by impaired stress hematopoiesis, resulting in marked erythrocyte fragmentation and intravascular hemolysis, coagulation abnormalities, endothelial damage, and iron deposition in renal and hepatic tissues. Clinical features include persistent hemolytic anemia, asplenia, nephritis, generalized erythematous rash, growth retardation and hepatomegaly.<ref>PMID:9884342</ref> |
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/HMOX1_HUMAN HMOX1_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. | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Heme oxygenase]] | ||
| + | [[Category: Caaveiro, J M.M]] | ||
[[Category: Morante, K]] | [[Category: Morante, K]] | ||
| + | [[Category: Sigala, P]] | ||
[[Category: Tsumoto, K]] | [[Category: Tsumoto, K]] | ||
| + | [[Category: Biliverdin biosensor]] | ||
| + | [[Category: Heme coordination]] | ||
| + | [[Category: Oxidoreductase]] | ||
| + | [[Category: Proximal histidine]] | ||
| + | [[Category: Site-directed mutagenesis]] | ||
Revision as of 11:19, 9 September 2015
Crystal structure of human HO1 H25R
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