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4a6p

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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=4a6p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a6p OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4a6p RCSB], [http://www.ebi.ac.uk/pdbsum/4a6p 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=4a6p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a6p OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4a6p RCSB], [http://www.ebi.ac.uk/pdbsum/4a6p PDBsum]</span></td></tr>
</table>
</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/RADA_PYRFU RADA_PYRFU]] Involved in DNA repair and in homologous recombination. Binds and assemble on single-stranded DNA to form a nucleoprotein filament. Hydrolyzes ATP in a ssDNA-dependent manner and promotes DNA strand exchange between homologous DNA molecules.
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</StructureSection>
</StructureSection>

Revision as of 17:17, 24 December 2014

RadA C-terminal ATPase domain from Pyrococcus furiosus

4a6p, resolution 1.50Å

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