1f2t
From Proteopedia
(Difference between revisions)
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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=1f2t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f2t OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1f2t RCSB], [http://www.ebi.ac.uk/pdbsum/1f2t 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=1f2t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f2t OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1f2t RCSB], [http://www.ebi.ac.uk/pdbsum/1f2t PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[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] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 19:41, 24 December 2014
Crystal Structure of ATP-Free RAD50 ABC-ATPase
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