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3v7j
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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=3v7j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v7j OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3v7j RCSB], [http://www.ebi.ac.uk/pdbsum/3v7j 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=3v7j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v7j OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3v7j RCSB], [http://www.ebi.ac.uk/pdbsum/3v7j PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/DPOLB_RAT DPOLB_RAT]] Repair polymerase that plays a key role in base-excision repair. Has 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity that removes the 5' sugar phosphate and also acts as a DNA polymerase that adds one nucleotide to the 3' end of the arising single-nucleotide gap. Conducts 'gap-filling' DNA synthesis in a stepwise distributive fashion rather than in a processive fashion as for other DNA polymerases. | ||
==See Also== | ==See Also== | ||
Revision as of 09:29, 25 December 2014
Co-crystal structure of Wild Type Rat polymerase beta: Enzyme-DNA binary complex
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