2ji2
From Proteopedia
(Difference between revisions)
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<StructureSection load='2ji2' size='340' side='right' caption='[[2ji2]], [[Resolution|resolution]] 1.70Å' scene=''> | <StructureSection load='2ji2' size='340' side='right' caption='[[2ji2]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2ji2]] is a 4 chain structure | + | <table><tr><td colspan='2'>[[2ji2]] is a 4 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2JI2 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>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></td></tr> | </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>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1vzg|1vzg]], [[1vzh|1vzh]], [[1vzi|1vzi]], [[2ji1|2ji1]], [[2ji3|2ji3]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1vzg|1vzg]], [[1vzh|1vzh]], [[1vzi|1vzi]], [[2ji1|2ji1]], [[2ji3|2ji3]]</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='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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ji2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ji2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ji2 RCSB], [http://www.ebi.ac.uk/pdbsum/2ji2 PDBsum]</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=2ji2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ji2 OCA], [http://pdbe.org/2ji2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ji2 RCSB], [http://www.ebi.ac.uk/pdbsum/2ji2 PDBsum]</span></td></tr> |
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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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 2ji2" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Desulfarculus baarsii]] | ||
[[Category: Superoxide reductase]] | [[Category: Superoxide reductase]] | ||
[[Category: Adam, V]] | [[Category: Adam, V]] | ||
Revision as of 12:09, 11 September 2015
X-RAY STRUCTURE OF E114A MUTANT OF SUPEROXIDE REDUCTASE FROM DESULFOARCULUS BAARSII IN THE NATIVE, REDUCED FORM
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Categories: Superoxide reductase | Adam, V | Amara, P | Bourgeois, D | Carpentier, P | Katona, G | Niviere, V | Ohana, J | Tsanov, N | Detoxification | Electron transport | Intermediate trapping | Iron | Metal-binding | Microspectrophotometry | Oxidoreductase | Raman spectroscopy | Redox state | Transport
