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3tkr

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<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=3tkr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tkr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3tkr RCSB], [http://www.ebi.ac.uk/pdbsum/3tkr PDBsum]</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=3tkr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tkr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3tkr RCSB], [http://www.ebi.ac.uk/pdbsum/3tkr PDBsum]</span></td></tr>
</table>
</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/PRDX4_HUMAN PRDX4_HUMAN]] Probably involved in redox regulation of the cell. Regulates the activation of NF-kappa-B in the cytosol by a modulation of I-kappa-B-alpha phosphorylation.<ref>PMID:9388242</ref>
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==

Revision as of 21:48, 25 December 2014

Crystal structure of full-length human peroxiredoxin 4 with T118E mutation

3tkr, resolution 2.10Å

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