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4ea5

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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=4ea5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ea5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ea5 RCSB], [http://www.ebi.ac.uk/pdbsum/4ea5 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=4ea5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ea5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ea5 RCSB], [http://www.ebi.ac.uk/pdbsum/4ea5 PDBsum]</span></td></tr>
</table>
</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/MBD4_HUMAN MBD4_HUMAN]] Mismatch-specific DNA N-glycosylase involved in DNA repair. Has thymine glycosylase activity and is specific for G:T mismatches within methylated and unmethylated CpG sites. Can also remove uracil or 5-fluorouracil in G:U mismatches. Has no lyase activity. Was first identified as methyl-CpG-binding protein.<ref>PMID:10097147</ref> <ref>PMID:10930409</ref>
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==

Revision as of 17:28, 24 December 2014

Structure of the glycoslyase domain of MBD4 bound to a 5hmU containing DNA

4ea5, resolution 2.14Å

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