4wmh
From Proteopedia
(Difference between revisions)
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==Structure of heme oxygenase-2 containing residues 1-288 lacking the membrane spanning region== | ==Structure of heme oxygenase-2 containing residues 1-288 lacking the membrane spanning region== | ||
| - | <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 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> | <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> | ||
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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. | ||
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| + | ==See Also== | ||
| + | *[[Heme oxygenase 3D structures|Heme oxygenase 3D structures]] | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Heme oxygenase]] | [[Category: Heme oxygenase]] | ||
[[Category: Human]] | [[Category: Human]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Bianchetti, C M]] | [[Category: Bianchetti, C M]] | ||
[[Category: Structural genomic]] | [[Category: Structural genomic]] | ||
Revision as of 08:40, 4 December 2019
Structure of heme oxygenase-2 containing residues 1-288 lacking the membrane spanning region
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