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2r37
From Proteopedia
(Difference between revisions)
(New page: 200px<br /> <applet load="2r37" size="450" color="white" frame="true" align="right" spinBox="true" caption="2r37, resolution 1.85Å" /> '''Crystal structure o...) |
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| - | [[Image:2r37.gif|left|200px]]<br /> | ||
| - | <applet load="2r37" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2r37, resolution 1.85Å" /> | ||
| - | '''Crystal structure of human glutathione peroxidase 3 (selenocysteine to glycine mutant)'''<br /> | ||
| - | == | + | ==Crystal structure of human glutathione peroxidase 3 (selenocysteine to glycine mutant)== |
| - | + | <StructureSection load='2r37' size='340' side='right'caption='[[2r37]], [[Resolution|resolution]] 1.85Å' scene=''> | |
| - | [ | + | == Structural highlights == |
| - | [[ | + | <table><tr><td colspan='2'>[[2r37]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2R37 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2R37 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]] 1.85Å</td></tr> |
| - | [[ | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=2r37 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2r37 OCA], [https://pdbe.org/2r37 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2r37 RCSB], [https://www.ebi.ac.uk/pdbsum/2r37 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2r37 ProSAT]</span></td></tr> | |
| - | [ | + | </table> |
| - | + | == Function == | |
| - | [ | + | [https://www.uniprot.org/uniprot/GPX3_HUMAN GPX3_HUMAN] Protects cells and enzymes from oxidative damage, by catalyzing the reduction of hydrogen peroxide, lipid peroxides and organic hydroperoxide, by glutathione. |
| - | [ | + | == 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/r3/2r37_consurf.spt"</scriptWhenChecked> | |
| - | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=2r37 ConSurf]. | |
| - | + | <div style="clear:both"></div> | |
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| - | + | ==See Also== | |
| + | *[[Glutathione peroxidase|Glutathione peroxidase]] | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Arrowsmith CH]] | ||
| + | [[Category: Edwards AM]] | ||
| + | [[Category: Gileadi O]] | ||
| + | [[Category: Guo K]] | ||
| + | [[Category: Johannson C]] | ||
| + | [[Category: Kavanagh KL]] | ||
| + | [[Category: Oppermann U]] | ||
| + | [[Category: Pike ACW]] | ||
| + | [[Category: Pilka ES]] | ||
| + | [[Category: Rojkowa A]] | ||
| + | [[Category: Sundstrom M]] | ||
| + | [[Category: Weigelt J]] | ||
| + | [[Category: Von Delft F]] | ||
Current revision
Crystal structure of human glutathione peroxidase 3 (selenocysteine to glycine mutant)
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Categories: Homo sapiens | Large Structures | Arrowsmith CH | Edwards AM | Gileadi O | Guo K | Johannson C | Kavanagh KL | Oppermann U | Pike ACW | Pilka ES | Rojkowa A | Sundstrom M | Weigelt J | Von Delft F
