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[[Image:1srd.jpg|left|200px]]
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{{STRUCTURE_1srd|  PDB=1srd  |  SCENE=  }}
'''THREE-DIMENSIONAL STRUCTURE OF CU,ZN-SUPEROXIDE DISMUTASE FROM SPINACH AT 2.0 ANGSTROMS RESOLUTION'''


==Three-dimensional structure of CU,ZN-superoxide dismutase from spinach at 2.0 Angstroms resolution==
<StructureSection load='1srd' size='340' side='right'caption='[[1srd]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1srd]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Spinacia_oleracea Spinacia oleracea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SRD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SRD FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=1srd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1srd OCA], [https://pdbe.org/1srd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1srd RCSB], [https://www.ebi.ac.uk/pdbsum/1srd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1srd ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SODCP_SPIOL SODCP_SPIOL] Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/sr/1srd_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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/main_output.php?pdb_ID=1srd ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The three-dimensional structure of Cu,Zn-superoxide dismutase from spinach leaves has been determined by X-ray crystal structure analysis. The atomic coordinates were refined at 2.0 A resolution using the Hendrickson and Konnert program for stereochemically restrained refinement against structure factors, which allowed the use of non-crystallographic symmetry. The crystallographic residual error for the refined model was 24.9%, with a root mean square deviation of 0.03 A from the ideal bond length and an average atomic temperature factor of 9.6 A. A dimeric molecule of the enzyme is comprised of two identical subunits related by a non-crystallographic 2-fold axis. Each subunit of 154 amino acid residues is composed primarily of eight anti-parallel beta-strands that form a flattened cylinder, plus three external loops. The main-chain hydrogen bonds primarily link the beta-strands. The overall structure of this enzyme is quite similar to that of the bovine dismutase except for some parts. The single disulfide bridge (Cys57-Cys146) and the salt bridge (Arg79-Asp101) may stabilize the loop regions of the structure. The Cu2+ and Zn2+ ions in the active site lie 6.1 A apart at the bottom of the long channel. The Cu2+ ligands (ND1 of His-46, and NE2 of His-48, -63, and -120) show an uneven tetrahedral distortion from a square plane. The Zn2+ ligands (ND1 of His-63, -71, and -80 and OD1 of Asp-83) show an almost tetrahedral geometry. The imidazole ring of His-63 forms a bridge between the Cu2+ and Zn2+ ions.(ABSTRACT TRUNCATED AT 250 WORDS)


==Overview==
Three-dimensional structure of Cu,Zn-superoxide dismutase from spinach at 2.0 A resolution.,Kitagawa Y, Tanaka N, Hata Y, Kusunoki M, Lee GP, Katsube Y, Asada K, Aibara S, Morita Y J Biochem. 1991 Mar;109(3):477-85. PMID:1880134<ref>PMID:1880134</ref>
The three-dimensional structure of Cu,Zn-superoxide dismutase from spinach leaves has been determined by X-ray crystal structure analysis. The atomic coordinates were refined at 2.0 A resolution using the Hendrickson and Konnert program for stereochemically restrained refinement against structure factors, which allowed the use of non-crystallographic symmetry. The crystallographic residual error for the refined model was 24.9%, with a root mean square deviation of 0.03 A from the ideal bond length and an average atomic temperature factor of 9.6 A. A dimeric molecule of the enzyme is comprised of two identical subunits related by a non-crystallographic 2-fold axis. Each subunit of 154 amino acid residues is composed primarily of eight anti-parallel beta-strands that form a flattened cylinder, plus three external loops. The main-chain hydrogen bonds primarily link the beta-strands. The overall structure of this enzyme is quite similar to that of the bovine dismutase except for some parts. The single disulfide bridge (Cys57-Cys146) and the salt bridge (Arg79-Asp101) may stabilize the loop regions of the structure. The Cu2+ and Zn2+ ions in the active site lie 6.1 A apart at the bottom of the long channel. The Cu2+ ligands (ND1 of His-46, and NE2 of His-48, -63, and -120) show an uneven tetrahedral distortion from a square plane. The Zn2+ ligands (ND1 of His-63, -71, and -80 and OD1 of Asp-83) show an almost tetrahedral geometry. The imidazole ring of His-63 forms a bridge between the Cu2+ and Zn2+ ions.(ABSTRACT TRUNCATED AT 250 WORDS)


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1SRD is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Spinacia_oleracea Spinacia oleracea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SRD OCA].
</div>
<div class="pdbe-citations 1srd" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Three-dimensional structure of Cu,Zn-superoxide dismutase from spinach at 2.0 A resolution., Kitagawa Y, Tanaka N, Hata Y, Kusunoki M, Lee GP, Katsube Y, Asada K, Aibara S, Morita Y, J Biochem. 1991 Mar;109(3):477-85. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1880134 1880134]
*[[Superoxide dismutase 3D structures|Superoxide dismutase 3D structures]]
[[Category: Single protein]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Spinacia oleracea]]
[[Category: Spinacia oleracea]]
[[Category: Superoxide dismutase]]
[[Category: Katsube Y]]
[[Category: Katsube, Y.]]
[[Category: Kitagawa Y]]
[[Category: Kitagawa, Y.]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 09:03:33 2008''
Retrieved from "https://proteopedia.org/1srd"