3sdp

<StructureSection load='3sdp' size='340' side='right' caption='[[3sdp]], [[Resolution|resolution]] 2.10&Aring;' scene=''>

<table><tr><td colspan='2'>[[3sdp]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_fluorescens_putidus"_flugge_1886 "bacillus fluorescens putidus" flugge 1886]. 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=3SDP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SDP FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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'>[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=3sdp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sdp OCA], [http://pdbe.org/3sdp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3sdp RCSB], [http://www.ebi.ac.uk/pdbsum/3sdp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3sdp ProSAT]</span></td></tr>

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

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== Publication Abstract from PubMed ==

The 2.1-A resolution crystal structure of native uncomplexed iron superoxide dismutase (EC 1.15.1.1) from Pseudomonas ovalis was solved and refined to a final R factor of 24%. The dimeric structure contains one catalytic iron center per monomer with an asymmetric trigonal-bipyramidal coordination of protein ligands to the metal. Each monomer contains two domains, with the trigonal ligands (histidines 74 and 160; aspartate 156) contributed by the large domain and stabilized by an extended hydrogen-bonded network, including residues from opposing monomers. The axial ligand (histidine 26) is found on the small domain and does not participate extensively in the stabilizing H-bond network. The open axial coordination position of the iron is devoid of bound water molecules or anions. The metal is located 0.5 A out of the plane of the trigonal ligands toward histidine 26, providing a slightly skewed coordination away from the iron binding site. The molecule contains a glutamine residue in the active site which is conserved between all iron enzymes sequenced to data but which is conserved among all manganese SODs at a separate position in the sequence. This residue shows the same structural interactions in both cases, implying that iron and manganese SODs are second-site revertants of one another.

The 2.1-A resolution structure of iron superoxide dismutase from Pseudomonas ovalis.,Stoddard BL, Howell PL, Ringe D, Petsko GA Biochemistry. 1990 Sep 25;29(38):8885-93. PMID:2271564<ref>PMID:2271564</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 3sdp" style="background-color:#fffaf0;"></div>

*[[Superoxide Dismutase|Superoxide Dismutase]]

[[Category: Bacillus fluorescens putidus flugge 1886]]

[[Category: Petsko, G A]]

[[Category: Ringe, D]]

[[Category: Stoddard, B L]]