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4hd0

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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=4hd0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hd0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4hd0 RCSB], [http://www.ebi.ac.uk/pdbsum/4hd0 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=4hd0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hd0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4hd0 RCSB], [http://www.ebi.ac.uk/pdbsum/4hd0 PDBsum]</span></td></tr>
</table>
</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/MRE11_PYRFU MRE11_PYRFU]] Involved in DNA double-strand break repair (DSBR). The Rad50/Mre11 complex possesses single-strand endonuclease activity and ATP-dependent double-strand-specific 3'-5' exonuclease activity.
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==

Revision as of 23:17, 24 December 2014

Mre11 ATLD17/18 mutation retains Tel1/ATM activity but blocks DNA double-strand break repair

4hd0, resolution 2.30Å

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