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4ymm
From Proteopedia
(Difference between revisions)
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<StructureSection load='4ymm' size='340' side='right'caption='[[4ymm]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='4ymm' size='340' side='right'caption='[[4ymm]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[4ymm]] is a 4 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[4ymm]] 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=4YMM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YMM FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=7BG:2-AMINO-7-BENZYL-9-(2-DEOXY-2-FLUORO-5-O-PHOSPHONO-BETA-D-ARABINOFURANOSYL)-6-OXO-6,9-DIHYDRO-1H-PURIN-7-IUM'>7BG</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=4ymm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ymm OCA], [https://pdbe.org/4ymm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ymm RCSB], [https://www.ebi.ac.uk/pdbsum/4ymm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ymm ProSAT]</span></td></tr> | |
| - | + | ||
| - | + | ||
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== Function == | == 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> |
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Homo sapiens]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Koag | + | [[Category: Koag M-C]] |
| - | [[Category: Lee | + | [[Category: Lee S]] |
| - | + | ||
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Revision as of 08:19, 3 May 2023
Structure of human DNA polymerase beta complexed with 7BG as the template base in a 1-nucleotide gapped DNA
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