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5b6m
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==Crystal structure of human peroxiredoxin 6 in reduced state== | ==Crystal structure of human peroxiredoxin 6 in reduced state== | ||
| - | <StructureSection load='5b6m' size='340' side='right' caption='[[5b6m]], [[Resolution|resolution]] 2.50Å' scene=''> | + | <StructureSection load='5b6m' size='340' side='right'caption='[[5b6m]], [[Resolution|resolution]] 2.50Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5b6m]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5B6M OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[5b6m]] is a 6 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=5B6M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5B6M FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.496Å</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=5b6m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b6m OCA], [https://pdbe.org/5b6m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5b6m RCSB], [https://www.ebi.ac.uk/pdbsum/5b6m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5b6m ProSAT]</span></td></tr> | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/PRDX6_HUMAN PRDX6_HUMAN] Involved in redox regulation of the cell. Can reduce H(2)O(2) and short chain organic, fatty acid, and phospholipid hydroperoxides. May play a role in the regulation of phospholipid turnover as well as in protection against oxidative injury. |
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 5b6m" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5b6m" style="background-color:#fffaf0;"></div> | ||
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| + | ==See Also== | ||
| + | *[[Peroxiredoxin 3D structures|Peroxiredoxin 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Homo sapiens]] |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Kim | + | [[Category: Kim EE]] |
| - | [[Category: | + | [[Category: Kim KH]] |
| - | [[Category: | + | [[Category: Lee WT]] |
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Current revision
Crystal structure of human peroxiredoxin 6 in reduced state
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Categories: Homo sapiens | Large Structures | Kim EE | Kim KH | Lee WT
