1q0d

<StructureSection load='1q0d' size='340' side='right' caption='[[1q0d]], [[Resolution|resolution]] 2.20&Aring;' scene=''>

<table><tr><td colspan='2'>[[1q0d]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptomyces_seoulensis Streptomyces seoulensis]. The October 2007 RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Superoxide Dismutase'' by David S. Goodsell is [http://dx.doi.org/10.2210/rcsb_pdb/mom_2007_10 10.2210/rcsb_pdb/mom_2007_10]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q0D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1Q0D FirstGlance]. <br>

</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=3NI:NICKEL+(III)+ION'>3NI</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br>

<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1q0f|1q0f]], [[1q0g|1q0g]], [[1q0k|1q0k]], [[1q0m|1q0m]]</td></tr>

<tr><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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1q0d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q0d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1q0d RCSB], [http://www.ebi.ac.uk/pdbsum/1q0d PDBsum]</span></td></tr>

<table>

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/q0/1q0d_consurf.spt"</scriptWhenChecked>

</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].

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

Superoxide dismutases (SODs, EC 1.15.1.1) are ubiquitous enzymes that efficiently catalyze the dismutation of superoxide radical anions to protect biological molecules from oxidative damage. The crystal structure of nickel-containing SOD (NiSOD) from Streptomyces seoulensis was determined for the resting, x-ray-reduced, and thiosulfate-reduced enzyme state. NiSOD is a homohexamer consisting of four-helix-bundle subunits. The catalytic center resides in the N-terminal active-site loop, where a Ni(III) ion is coordinated by the amino group of His-1, the amide group of Cys-2, two thiolate groups of Cys-2 and Cys-6, and the imidazolate of His-1 as axial ligand that is lost in the chemically reduced state as well as after x-ray-induced reduction. This structure represents a third class of SODs concerning the catalytic metal species, subunit structure, and oligomeric organization. It adds a member to the small number of Ni-metalloenzymes and contributes with its Ni(III) active site to the general understanding of Ni-related biochemistry. NiSOD is shown to occur also in bacteria other than Streptomyces and is predicted to be present in some cyanobacteria.

Crystal structure of nickel-containing superoxide dismutase reveals another type of active site.,Wuerges J, Lee JW, Yim YI, Yim HS, Kang SO, Djinovic Carugo K Proc Natl Acad Sci U S A. 2004 Jun 8;101(23):8569-74. Epub 2004 Jun 1. PMID:15173586<ref>PMID:15173586</ref>

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

</div>

*[[Superoxide Dismutase|Superoxide Dismutase]]

[[Category: Superoxide dismutase]]

[[Category: Carugo, K Djinovic.]]

[[Category: Kang, S O.]]

[[Category: Lee, J W.]]

[[Category: Wuerges, J.]]

[[Category: Yim, H S.]]

[[Category: Yim, Y I.]]

[[Category: Oxidoreductase]]