4wmh: Difference between revisions
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<StructureSection load='4wmh' size='340' side='right' caption='[[4wmh]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='4wmh' size='340' side='right' caption='[[4wmh]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4wmh]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WMH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WMH FirstGlance]. <br> | <table><tr><td colspan='2'>[[4wmh]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WMH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WMH FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2qpp|2qpp]], [[2rgz|2rgz]], [[2q32|2q32]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2qpp|2qpp]], [[2rgz|2rgz]], [[2q32|2q32]]</td></tr> | ||
<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 HUMAN])</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='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=4wmh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wmh OCA], [http://pdbe.org/4wmh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4wmh RCSB], [http://www.ebi.ac.uk/pdbsum/4wmh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4wmh ProSAT]</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=4wmh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wmh OCA], [http://pdbe.org/4wmh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4wmh RCSB], [http://www.ebi.ac.uk/pdbsum/4wmh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4wmh ProSAT]</span></td></tr> | ||
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== Function == | == Function == | ||
[[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. | [[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. | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Heme oxygenase]] | [[Category: Heme oxygenase]] | ||
[[Category: Human]] | |||
[[Category: Bianchetti, C M]] | [[Category: Bianchetti, C M]] | ||
[[Category: Structural genomic]] | [[Category: Structural genomic]] | ||
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[[Category: Cesg]] | [[Category: Cesg]] | ||
[[Category: Ho2]] | [[Category: Ho2]] | ||
[[Category: Oxidoreductase]] | |||
[[Category: Oxygenase]] | [[Category: Oxygenase]] | ||
[[Category: PSI, Protein structure initiative]] | [[Category: PSI, Protein structure initiative]] | ||