1t5p: Difference between revisions

<StructureSection load='1t5p' size='340' side='right'caption='[[1t5p]], [[Resolution|resolution]] 2.11&Aring;' scene=''>

<table><tr><td colspan='2'>[[1t5p]] is a 2 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=1T5P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1T5P FirstGlance]. <br>

</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.11&#8491;</td></tr>

<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1FH:12-PHENYLHEME'>1FH</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=1t5p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t5p OCA], [https://pdbe.org/1t5p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1t5p RCSB], [https://www.ebi.ac.uk/pdbsum/1t5p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1t5p ProSAT]</span></td></tr>

[https://www.uniprot.org/uniprot/HMOX1_HUMAN HMOX1_HUMAN] Defects in HMOX1 are the cause of heme oxygenase 1 deficiency (HMOX1D) [MIM:[https://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>  

[https://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.

*[[Heme oxygenase 3D structures|Heme oxygenase 3D structures]]

[[Category: Homo sapiens]]

[[Category: Large Structures]]

[[Category: Buldain G]]

[[Category: Lad L]]

[[Category: Niemevz F]]

[[Category: Ortiz de Montellano PR]]

[[Category: Poulos TL]]

[[Category: Wang J]]