6crh: Difference between revisions

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-'''Unreleased structure'''
-The entry 6crh is ON HOLD  until Paper Publication
+==Structure of human DNA polymerase beta complexed with 8-ClG in the template base paired with incoming non-hydrolyzable GTP==
+<StructureSection load='6crh' size='340' side='right'caption='[[6crh]], [[Resolution|resolution]] 2.33&Aring;' scene=''>
-Authors: Koag, M.-C., Lee, S.
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6crh]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CRH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6CRH FirstGlance]. <br>
-Description: Structure of human DNA polymerase beta complexed with 8-ClG in the template base paired with incoming non-hydrolyzable GTP
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=XG4:2-DEOXY-5-O-[(R)-HYDROXY{[(R)-HYDROXY(PHOSPHONOOXY)PHOSPHORYL]AMINO}PHOSPHORYL]GUANOSINE'>XG4</scene></td></tr>
-[[Category: Unreleased Structures]]
+<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=F74:'>F74</scene></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=6crh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6crh OCA], [http://pdbe.org/6crh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6crh RCSB], [http://www.ebi.ac.uk/pdbsum/6crh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6crh ProSAT]</span></td></tr>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/DPOLB_HUMAN DPOLB_HUMAN]] 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.<ref>PMID:9207062</ref> <ref>PMID:9572863</ref> <ref>PMID:11805079</ref> <ref>PMID:21362556</ref>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Koag, M C]]
 [[Category: Lee, S]]
-[[Category: Koag, M.-C]]
+[[Category: Dna binding protein]]
+[[Category: Lyase-dna complex]]
+[[Category: Transferase]]