1ix4

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[[Image:1ix4.png|left|200px]]
 
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{{STRUCTURE_1ix4| PDB=1ix4 | SCENE= }}
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==Crystal Structure of Rat Heme Oxygenase-1 in complex with Heme bound to Carbon Monoxide==
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<StructureSection load='1ix4' size='340' side='right'caption='[[1ix4]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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===Crystal Structure of Rat Heme Oxygenase-1 in complex with Heme bound to Carbon Monoxide===
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1ix4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IX4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IX4 FirstGlance]. <br>
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{{ABSTRACT_PUBMED_12924938}}
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CMO:CARBON+MONOXIDE'>CMO</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
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==About this Structure==
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ix4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ix4 OCA], [https://pdbe.org/1ix4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ix4 RCSB], [https://www.ebi.ac.uk/pdbsum/1ix4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ix4 ProSAT]</span></td></tr>
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[[1ix4]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IX4 OCA].
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</table>
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== Function ==
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[https://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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ix/1ix4_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ix4 ConSurf].
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<div style="clear:both"></div>
==See Also==
==See Also==
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*[[Heme oxygenase|Heme oxygenase]]
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*[[Heme oxygenase 3D structures|Heme oxygenase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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<ref group="xtra">PMID:012924938</ref><references group="xtra"/>
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[[Category: Large Structures]]
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[[Category: Heme oxygenase]]
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[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Fukuyama, K.]]
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[[Category: Fukuyama K]]
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[[Category: Hayashi, S.]]
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[[Category: Hayashi S]]
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[[Category: Noguchi, M.]]
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[[Category: Noguchi M]]
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[[Category: Omata, Y.]]
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[[Category: Omata Y]]
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[[Category: Sakamoto, H.]]
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[[Category: Sakamoto H]]
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[[Category: Sugishima, M.]]
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[[Category: Sugishima M]]
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[[Category: Hemeprotein]]
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[[Category: Inhibitor complex]]
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[[Category: Oxidoreductase]]
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Current revision

Crystal Structure of Rat Heme Oxygenase-1 in complex with Heme bound to Carbon Monoxide

PDB ID 1ix4

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