3qkr

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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=3qkr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qkr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3qkr RCSB], [http://www.ebi.ac.uk/pdbsum/3qkr 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=3qkr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qkr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3qkr RCSB], [http://www.ebi.ac.uk/pdbsum/3qkr PDBsum]</span></td></tr>
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== Function ==
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[[http://www.uniprot.org/uniprot/RAD50_PYRFU RAD50_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. Rad50 provides an ATP-dependent control of Mre11 by unwinding and/or repositioning DNA ends into the Mre11 active site.[HAMAP-Rule:MF_00449] [[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 18:19, 25 December 2014

Mre11 Rad50 binding domain bound to Rad50

3qkr, resolution 3.40Å

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