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2ji2

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Current revision (14:49, 13 December 2023) (edit) (undo)
 
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<StructureSection load='2ji2' size='340' side='right'caption='[[2ji2]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
<StructureSection load='2ji2' size='340' side='right'caption='[[2ji2]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2ji2]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_33931 Atcc 33931]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JI2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JI2 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2ji2]] 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=2JI2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JI2 FirstGlance]. <br>
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</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>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></td></tr>
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</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>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1vzg|1vzg]], [[1vzh|1vzh]], [[1vzi|1vzi]], [[2ji1|2ji1]], [[2ji3|2ji3]]</div></td></tr>
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<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>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dfx, rbo, Deba_2050 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=453230 ATCC 33931])</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Superoxide_reductase Superoxide reductase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.15.1.2 1.15.1.2] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ji2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ji2 OCA], [https://pdbe.org/2ji2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ji2 RCSB], [https://www.ebi.ac.uk/pdbsum/2ji2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ji2 ProSAT]</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=2ji2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ji2 OCA], [https://pdbe.org/2ji2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ji2 RCSB], [https://www.ebi.ac.uk/pdbsum/2ji2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ji2 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[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>
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[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]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Atcc 33931]]
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[[Category: Desulfarculus baarsii]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Superoxide reductase]]
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[[Category: Adam V]]
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[[Category: Adam, V]]
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[[Category: Amara P]]
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[[Category: Amara, P]]
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[[Category: Bourgeois D]]
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[[Category: Bourgeois, D]]
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[[Category: Carpentier P]]
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[[Category: Carpentier, P]]
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[[Category: Katona G]]
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[[Category: Katona, G]]
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[[Category: Niviere V]]
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[[Category: Niviere, V]]
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[[Category: Ohana J]]
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[[Category: Ohana, J]]
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[[Category: Tsanov N]]
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[[Category: Tsanov, N]]
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[[Category: Detoxification]]
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[[Category: Electron transport]]
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[[Category: Intermediate trapping]]
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[[Category: Iron]]
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[[Category: Metal-binding]]
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[[Category: Microspectrophotometry]]
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[[Category: Oxidoreductase]]
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[[Category: Raman spectroscopy]]
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[[Category: Redox state]]
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[[Category: Transport]]
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Current revision

X-ray structure of E114A mutant of superoxide reductase from Desulfoarculus baarsii in the native, reduced form

PDB ID 2ji2

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