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==X-RAY STRUCTURE OF WILD-TYPE SUPEROXIDE REDUCTASE FROM DESULFOARCULUS BAARSII==
 
<StructureSection load='2ji1' size='340' side='right' caption='[[2ji1]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
==X-ray structure of wild-type superoxide reductase from Desulfoarculus baarsii==
<StructureSection load='2ji1' size='340' side='right'caption='[[2ji1]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2ji1]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Desulfarculus_baarsii Desulfarculus baarsii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JI1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2JI1 FirstGlance]. <br>
<table><tr><td colspan='2'>[[2ji1]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Desulfarculus_baarsii Desulfarculus baarsii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JI1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JI1 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1vzg|1vzg]], [[1vzh|1vzh]], [[1vzi|1vzi]], [[2ji2|2ji2]], [[2ji3|2ji3]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Superoxide_reductase Superoxide reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.15.1.2 1.15.1.2] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ji1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ji1 OCA], [https://pdbe.org/2ji1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ji1 RCSB], [https://www.ebi.ac.uk/pdbsum/2ji1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ji1 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=2ji1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ji1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ji1 RCSB], [http://www.ebi.ac.uk/pdbsum/2ji1 PDBsum]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/DFX_DESB2 DFX_DESB2] Catalyzes the one-electron reduction of superoxide anion radical to hydrogen peroxide at a nonheme ferrous iron center. Plays a fundamental role in case of oxidative stress via its superoxide detoxification activity.<ref>PMID:10617593</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ji/2ji1_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ji/2ji1_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2ji1 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 2ji1" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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</StructureSection>
</StructureSection>
[[Category: Desulfarculus baarsii]]
[[Category: Desulfarculus baarsii]]
[[Category: Superoxide reductase]]
[[Category: Large Structures]]
[[Category: Adam, V]]
[[Category: Adam V]]
[[Category: Amara, P]]
[[Category: Amara P]]
[[Category: Bourgeois, D]]
[[Category: Bourgeois D]]
[[Category: Carpentier, P]]
[[Category: Carpentier P]]
[[Category: Katona, G]]
[[Category: Katona G]]
[[Category: Niviere, V]]
[[Category: Niviere V]]
[[Category: Ohana, J]]
[[Category: Ohana J]]
[[Category: Tsanov, N]]
[[Category: Tsanov N]]
[[Category: Detoxification]]
[[Category: Electron transport]]
[[Category: Intermediate trapping]]
[[Category: Iron]]
[[Category: Metal-binding]]
[[Category: Microspectrophotometry]]
[[Category: Oxidoreductase]]
[[Category: Raman spectroscopy]]
[[Category: Redox state]]
[[Category: Transport]]

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