2qpp

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|GENE= HMOX2, HO2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
|GENE= HMOX2, HO2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
|DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=cd00232 HemeO]</span>
|DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=cd00232 HemeO]</span>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2qpp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qpp OCA], [http://www.ebi.ac.uk/pdbsum/2qpp PDBsum], [http://www.fli-leibniz.de/cgi-bin/ImgLib.pl?CODE=1kfv JenaLib], [http://www.rcsb.org/pdb/explore.do?structureId=2qpp RCSB]</span>
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|RELATEDENTRY=[[2q32|2Q32]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2qpp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qpp OCA], [http://www.ebi.ac.uk/pdbsum/2qpp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2qpp RCSB]</span>
}}
}}
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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 Wed Mar 26 06:43:39 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:51:52 2008''

Revision as of 01:51, 31 March 2008

Image:2qpp.jpg


PDB ID 2qpp

Drag the structure with the mouse to rotate
, resolution 2.610Å
Sites: and
Ligands:
Gene: HMOX2, HO2 (Homo sapiens)
Activity: Heme oxygenase, with EC number 1.14.99.3
Domains: HemeO
Related: 2Q32


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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


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

2QPP 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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