1dpi
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=1dpi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dpi OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1dpi RCSB], [http://www.ebi.ac.uk/pdbsum/1dpi 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=1dpi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dpi OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1dpi RCSB], [http://www.ebi.ac.uk/pdbsum/1dpi PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/DPO1_ECOLI DPO1_ECOLI]] In addition to polymerase activity, this DNA polymerase exhibits 3' to 5' and 5' to 3' exonuclease activity. It is able to utilize nicked circular duplex DNA as a template and can unwind the parental DNA strand from its template. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 16:48, 24 December 2014
STRUCTURE OF LARGE FRAGMENT OF ESCHERICHIA COLI DNA POLYMERASE I COMPLEXED WITH D/TMP
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