4mfc: Difference between revisions

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-'''Unreleased structure'''
-The entry 4mfc is ON HOLD
+==Structure of human DNA polymerase beta complexed with O6MG in the template base paired with incoming non-hydrolyzable CTP==
+<StructureSection load='4mfc' size='340' side='right'caption='[[4mfc]], [[Resolution|resolution]] 2.13&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4mfc]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MFC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MFC FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.13&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0KX:2-DEOXY-5-O-[(R)-HYDROXY{[(R)-HYDROXY(PHOSPHONOOXY)PHOSPHORYL]AMINO}PHOSPHORYL]CYTIDINE'>0KX</scene>, <scene name='pdbligand=6OG:6-O-METHYL+GUANOSINE-5-MONOPHOSPHATE'>6OG</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4mfc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mfc OCA], [https://pdbe.org/4mfc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4mfc RCSB], [https://www.ebi.ac.uk/pdbsum/4mfc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4mfc ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://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>
-Authors: Koag, M.C., Min, K., Monzingo, A.F., Lee, S.
+==See Also==
+*[[DNA polymerase 3D structures|DNA polymerase 3D structures]]
-Description: Structure of human DNA polymerase beta complexed with O6MG in the template base paired with incoming non-hydrolyzable CTP
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Koag MC]]
+[[Category: Lee S]]
+[[Category: Min K]]
+[[Category: Monzingo AF]]