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1sqe
From Proteopedia
(Difference between revisions)
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<StructureSection load='1sqe' size='340' side='right' caption='[[1sqe]], [[Resolution|resolution]] 1.50Å' scene=''> | <StructureSection load='1sqe' size='340' side='right' caption='[[1sqe]], [[Resolution|resolution]] 1.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1sqe]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1sqe]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"micrococcus_aureus"_(rosenbach_1884)_zopf_1885 "micrococcus aureus" (rosenbach 1884) zopf 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SQE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1SQE FirstGlance]. <br> |
| - | </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=1sqe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sqe OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1sqe RCSB], [http://www.ebi.ac.uk/pdbsum/1sqe PDBsum], [http://www.topsan.org/Proteins/MCSG/1sqe TOPSAN]</span></td></tr> | + | </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=1sqe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sqe OCA], [http://pdbe.org/1sqe PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1sqe RCSB], [http://www.ebi.ac.uk/pdbsum/1sqe PDBsum], [http://www.topsan.org/Proteins/MCSG/1sqe TOPSAN]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[http://www.uniprot.org/uniprot/ | + | [[http://www.uniprot.org/uniprot/HDOX2_STAAM HDOX2_STAAM]] Allows bacterial pathogens to use the host heme as an iron source. Catalyzes the oxidative degradation of the heme macrocyclic porphyrin ring to the oxo-bilirubin chromophore staphylobilin (a mixture of the linear tetrapyrroles 5-oxo-delta-bilirubin and 15-oxo-beta-bilirubin) in the presence of a suitable electron donor such as ascorbate or NADPH--cytochrome P450 reductase, with subsequent release of free iron.[HAMAP-Rule:MF_01272] |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
| + | <div class="pdbe-citations 1sqe" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Staphylococcus aureus]] | ||
[[Category: Joachimiak, A]] | [[Category: Joachimiak, A]] | ||
[[Category: Joachimiak, G]] | [[Category: Joachimiak, G]] | ||
Revision as of 01:23, 11 September 2015
1.5A Crystal Structure Of the protein PG130 from Staphylococcus aureus, Structural genomics
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