2q32

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[[Image:2q32.jpg|left|200px]]<br /><applet load="2q32" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2q32.jpg|left|200px]]
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caption="2q32, resolution 2.400&Aring;" />
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'''Crystal structure of human heme oxygenase-2 C127A (HO-2)'''<br />
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{{Structure
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|PDB= 2q32 |SIZE=350|CAPTION= <scene name='initialview01'>2q32</scene>, resolution 2.400&Aring;
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|SITE= <scene name='pdbsite=AC1:Oxn+Binding+Site+For+Residue+A+301'>AC1</scene> and <scene name='pdbsite=AC2:Oxn+Binding+Site+For+Residue+B+301'>AC2</scene>
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|LIGAND= <scene name='pdbligand=OXN:OXTOXYNOL-10'>OXN</scene>
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|ACTIVITY= [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]
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|GENE= Hs.284279, HMOX2, HO2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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}}
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'''Crystal structure of human heme oxygenase-2 C127A (HO-2)'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2Q32 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=OXN:'>OXN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Known structural/functional Sites: <scene name='pdbsite=AC1:Oxn+Binding+Site+For+Residue+A+301'>AC1</scene> and <scene name='pdbsite=AC2:Oxn+Binding+Site+For+Residue+B+301'>AC2</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Q32 OCA].
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2Q32 is a [[Single protein]] structure of 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=2Q32 OCA].
==Reference==
==Reference==
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Comparison of apo- and heme-bound crystal structures of a truncated human heme oxygenase-2., Bianchetti CM, Yi L, Ragsdale SW, Phillips GN Jr, J Biol Chem. 2007 Dec 28;282(52):37624-31. Epub 2007 Oct 26. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17965015 17965015]
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Comparison of apo- and heme-bound crystal structures of a truncated human heme oxygenase-2., Bianchetti CM, Yi L, Ragsdale SW, Phillips GN Jr, J Biol Chem. 2007 Dec 28;282(52):37624-31. Epub 2007 Oct 26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17965015 17965015]
[[Category: Heme oxygenase]]
[[Category: Heme oxygenase]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Wesenberg, G E.]]
[[Category: Wesenberg, G E.]]
[[Category: OXN]]
[[Category: OXN]]
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[[Category: center for eukaryotic structural genomics]]
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[[Category: center for eukaryotic structural genomic]]
[[Category: cesg]]
[[Category: cesg]]
[[Category: heme oxygenase]]
[[Category: heme oxygenase]]
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[[Category: structural genomics medical relevance]]
[[Category: structural genomics medical relevance]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:35:34 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:20:58 2008''

Revision as of 16:21, 20 March 2008

Image:2q32.jpg


PDB ID 2q32

Drag the structure with the mouse to rotate
, resolution 2.400Å
Sites: and
Ligands:
Gene: Hs.284279, HMOX2, HO2 (Homo sapiens)
Activity: Heme oxygenase, with EC number 1.14.99.3
Coordinates: save as pdb, mmCIF, xml



Crystal structure of human heme oxygenase-2 C127A (HO-2)


Overview

Heme oxygenase (HO) catalyzes the first step in the heme degradation pathway. The crystal structures of apo- and heme-bound truncated human HO-2 reveal a primarily alpha-helical architecture similar to that of human HO-1 and other known HOs. Proper orientation of heme in HO-2 is required for the regioselective oxidation of the alpha-mesocarbon. This is accomplished by interactions within the heme binding pocket, which is made up of two helices. The iron coordinating residue, His(45), resides on the proximal helix. The distal helix contains highly conserved glycine residues that allow the helix to flex and interact with the bound heme. Tyr(154), Lys(199), and Arg(203) orient the heme through direct interactions with the heme propionates. The rearrangements of side chains in heme-bound HO-2 compared with apoHO-2 further elucidate HO-2 heme interactions.

About this Structure

2Q32 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Comparison of apo- and heme-bound crystal structures of a truncated human heme oxygenase-2., Bianchetti CM, Yi L, Ragsdale SW, Phillips GN Jr, J Biol Chem. 2007 Dec 28;282(52):37624-31. Epub 2007 Oct 26. PMID:17965015

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