1sda

<StructureSection load='1sda' size='340' side='right' caption='[[1sda]], [[Resolution|resolution]] 2.50&Aring;' scene=''>

<table><tr><td colspan='2'>[[1sda]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Bovin Bovin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SDA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1SDA FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>

<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NIY:META-NITRO-TYROSINE'>NIY</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_dismutase Superoxide dismutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.15.1.1 1.15.1.1] </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=1sda FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sda OCA], [http://pdbe.org/1sda PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1sda RCSB], [http://www.ebi.ac.uk/pdbsum/1sda PDBsum]</span></td></tr>

[[http://www.uniprot.org/uniprot/SODC_BOVIN SODC_BOVIN]] Destroys radicals which are normally produced within the cells and which are toxic to biological systems.

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/sd/1sda_consurf.spt"</scriptWhenChecked>

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== Publication Abstract from PubMed ==

The crystal structure of bovine Cu,Zn superoxide dismutase modified with peroxynitrite (ONOO-) was determined by X-ray diffraction, utilizing the existing three-dimensional model of the native structure deposited in the Brookhaven Protein Data Bank (J. A. Tainer et al., J. Mol. Biol. 160, 181-217, 1982). The native structure and the modified derivative were refined to R factors of 19.0 and 18.7% respectively using diffraction data from 6.0 to 2.5 A. The major result after reaction with peroxynitrite was the appearance of electron density 1.45 A from a single epsilon carbon of Tyr-108, the only tyrosine residue in the sequence. Tyr-108 is a solvent-exposed residue 18 A from the copper atom in the active site. The electron density was consistent with nitration of Tyr-108 at one of the epsilon carbons to form 3-nitrotyrosine. We propose that the nitration occurs in solution by transfer of a nitronium-like species from the active site on one superoxide dismutase dimer to the Tyr-108 of a second dimer.

Crystal structure of peroxynitrite-modified bovine Cu,Zn superoxide dismutase.,Smith CD, Carson M, van der Woerd M, Chen J, Ischiropoulos H, Beckman JS Arch Biochem Biophys. 1992 Dec;299(2):350-5. PMID:1444476<ref>PMID:1444476</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1sda" style="background-color:#fffaf0;"></div>

*[[Superoxide Dismutase|Superoxide Dismutase]]

[[Category: Bovin]]

[[Category: Superoxide dismutase]]

[[Category: Beckman, J S]]

[[Category: Carson, M]]

[[Category: Chen, J]]

[[Category: Ischiropoulos, H]]

[[Category: Smith, C D]]

[[Category: Woerd, M Van Der]]