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1srd

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(New page: 200px<br /><applet load="1srd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1srd, resolution 2.0&Aring;" /> '''THREE-DIMENSIONAL STR...)
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[[Image:1srd.jpg|left|200px]]<br /><applet load="1srd" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1srd, resolution 2.0&Aring;" />
 
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'''THREE-DIMENSIONAL STRUCTURE OF CU,ZN-SUPEROXIDE DISMUTASE FROM SPINACH AT 2.0 ANGSTROMS RESOLUTION'''<br />
 
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==Overview==
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==Three-dimensional structure of CU,ZN-superoxide dismutase from spinach at 2.0 Angstroms resolution==
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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)
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<StructureSection load='1srd' size='340' side='right'caption='[[1srd]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<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>
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</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>
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<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>
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<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>
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</table>
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== Function ==
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[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/sr/1srd_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1SRD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Spinacia_oleracea Spinacia oleracea] with CU and ZN as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SRD OCA].
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*[[Superoxide dismutase 3D structures|Superoxide dismutase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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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 (Tokyo). 1991 Mar;109(3):477-85. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=1880134 1880134]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Spinacia oleracea]]
[[Category: Spinacia oleracea]]
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[[Category: Superoxide dismutase]]
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[[Category: Katsube Y]]
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[[Category: Katsube, Y.]]
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[[Category: Kitagawa Y]]
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[[Category: Kitagawa, Y.]]
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[[Category: CU]]
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[[Category: ZN]]
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[[Category: oxidoreductase(superoxide acceptor)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 02:35:57 2007''
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Current revision

Three-dimensional structure of CU,ZN-superoxide dismutase from spinach at 2.0 Angstroms resolution

PDB ID 1srd

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