2rgz

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2rgz]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RGZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2RGZ FirstGlance]. <br>
<table><tr><td colspan='2'>[[2rgz]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RGZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2RGZ FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene><br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2qpp|2qpp]], [[2q32|2q32]]</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2qpp|2qpp]], [[2q32|2q32]]</td></tr>
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<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HMOX2, HO2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HMOX2, HO2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
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<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>
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<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>
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<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=2rgz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rgz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2rgz RCSB], [http://www.ebi.ac.uk/pdbsum/2rgz PDBsum]</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=2rgz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rgz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2rgz RCSB], [http://www.ebi.ac.uk/pdbsum/2rgz PDBsum]</span></td></tr>
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<table>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/HMOX2_HUMAN HMOX2_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 2 could be implicated in the production of carbon monoxide in brain where it could act as a neurotransmitter.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: Heme oxygenase]]
[[Category: Heme oxygenase]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Bianchetti, C M.]]
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[[Category: Bianchetti, C M]]
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[[Category: Bingman, C A.]]
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[[Category: Bingman, C A]]
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[[Category: Bitto, E.]]
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[[Category: Bitto, E]]
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[[Category: CESG, Center for Eukaryotic Structural Genomics.]]
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[[Category: Structural genomic]]
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[[Category: Phillips, G N.]]
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[[Category: Phillips, G N]]
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[[Category: Wesenberg, G E.]]
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[[Category: Wesenberg, G E]]
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[[Category: Center for eukaryotic structural genomic]]
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[[Category: Cesg]]
[[Category: Cesg]]
[[Category: Endoplasmic reticulum]]
[[Category: Endoplasmic reticulum]]
[[Category: Ensemble refinement]]
[[Category: Ensemble refinement]]
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[[Category: Heme oxygenase]]
 
[[Category: Ho-2]]
[[Category: Ho-2]]
[[Category: Iron]]
[[Category: Iron]]
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[[Category: Microsome]]
[[Category: Microsome]]
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]
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[[Category: Protein structure initiative]]
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[[Category: PSI, Protein structure initiative]]
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[[Category: Psi]]
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[[Category: Refinement methodology development]]
[[Category: Refinement methodology development]]
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[[Category: Structural genomic]]
 
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[[Category: Structural genomics community request]]
 
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[[Category: Structural genomics medical relevance]]
 

Revision as of 10:49, 25 December 2014

Ensemble refinement of the protein crystal structure of human heme oxygenase-2 C127A (HO-2) with bound heme

2rgz, resolution 2.61Å

Drag the structure with the mouse to rotate

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OCA

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