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3pih

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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=3pih FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pih OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3pih RCSB], [http://www.ebi.ac.uk/pdbsum/3pih 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=3pih FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pih OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3pih RCSB], [http://www.ebi.ac.uk/pdbsum/3pih PDBsum]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/UVRA_THEMA UVRA_THEMA]] The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrA is an ATPase and a DNA-binding protein. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. When the presence of a lesion has been verified by UvrB, the UvrA molecules dissociate (By similarity).
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==

Revision as of 03:00, 25 December 2014

T. maritima UvrA in complex with fluorescein-modified DNA

3pih, resolution 2.90Å

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