6j7i

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Current revision (10:02, 22 November 2023) (edit) (undo)
 
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<StructureSection load='6j7i' size='340' side='right'caption='[[6j7i]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
<StructureSection load='6j7i' size='340' side='right'caption='[[6j7i]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6j7i]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6J7I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6J7I FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6j7i]] is a 2 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=6J7I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6J7I FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
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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]] 3.3&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6j79|6j79]], [[6j7a|6j7a]]</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=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Por ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr>
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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=6j7i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6j7i OCA], [https://pdbe.org/6j7i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6j7i RCSB], [https://www.ebi.ac.uk/pdbsum/6j7i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6j7i ProSAT]</span></td></tr>
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<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=6j7i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6j7i OCA], [http://pdbe.org/6j7i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6j7i RCSB], [http://www.ebi.ac.uk/pdbsum/6j7i PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6j7i ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[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.
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[https://www.uniprot.org/uniprot/NCPR_RAT NCPR_RAT] This enzyme is required for electron transfer from NADP to cytochrome P450 in microsomes. It can also provide electron transfer to heme oxygenase and cytochrome B5.[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.
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 6j7i" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 6j7i" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Heme oxygenase 3D structures|Heme oxygenase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Buffalo rat]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Sato, H]]
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[[Category: Rattus norvegicus]]
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[[Category: Sugishima, M]]
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[[Category: Sato H]]
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[[Category: Wada, K]]
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[[Category: Sugishima M]]
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[[Category: Yamamoto, K]]
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[[Category: Wada K]]
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[[Category: Fusion protein]]
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[[Category: Yamamoto K]]
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[[Category: Oxidoreductase]]
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[[Category: Redox complex]]
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Current revision

Fusion protein of heme oxygenase-1 and NADPH cytochrome P450 reductase (15aa)

PDB ID 6j7i

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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