1vzh: Difference between revisions

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OCA

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 <StructureSection load='1vzh' size='340' side='right'caption='[[1vzh]], [[Resolution|resolution]] 1.69&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1vzh]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VZH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VZH FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1vzh]] is a 2 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=1VZH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VZH FirstGlance]. <br>
-</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=FC6:HEXACYANOFERRATE(3-)'>FC6</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</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]] 1.69&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1vzg|1vzg]], [[1vzi|1vzi]]</div></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=FC6:HEXACYANOFERRATE(3-)'>FC6</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr>
-<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>
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1vzh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vzh OCA], [https://pdbe.org/1vzh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vzh RCSB], [https://www.ebi.ac.uk/pdbsum/1vzh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vzh ProSAT]</span></td></tr>
 </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>
+[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 ==
 [[Image:Consurf_key_small.gif|200px|right]]
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 __TOC__
 </StructureSection>
+[[Category: Desulfarculus baarsii]]
 [[Category: Large Structures]]
-[[Category: Superoxide reductase]]
+[[Category: Adam V]]
-[[Category: Adam, V]]
+[[Category: Bourgeois D]]
-[[Category: Bourgeois, D]]
+[[Category: Molina-Heredia FP]]
-[[Category: Molina-Heredia, F P]]
+[[Category: Niviere V]]
-[[Category: Niviere, V]]
+[[Category: Royant A]]
-[[Category: Royant, A]]
-[[Category: Dinuclear iron cluster]]
-[[Category: Electron transport]]
-[[Category: Ferrocyanide]]
-[[Category: Microspectrophotometry]]
-[[Category: Oxidoreductase]]
-[[Category: Photoreduction]]
-[[Category: Redox state]]