This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
6c59
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==Chimeric Pol kappa RIR Rev1 C-terminal domain== | |
| - | + | <StructureSection load='6c59' size='340' side='right'caption='[[6c59]], [[Resolution|resolution]] 2.03Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[6c59]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6C59 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6C59 FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr> | |
| - | [[Category: | + | <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=6c59 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6c59 OCA], [http://pdbe.org/6c59 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6c59 RCSB], [http://www.ebi.ac.uk/pdbsum/6c59 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6c59 ProSAT]</span></td></tr> |
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/POLK_MOUSE POLK_MOUSE]] DNA polymerase specifically involved in DNA repair. Plays an important role in translesion synthesis, where the normal high-fidelity DNA polymerases cannot proceed and DNA synthesis stalls. Depending on the context, it inserts the correct base, but causes frequent base transitions, transversions and frameshifts. Lacks 3'-5' proofreading exonuclease activity. Forms a Schiff base with 5'-deoxyribose phosphate at abasic sites, but does not have lyase activity (By similarity).<ref>PMID:12432099</ref> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Wojtaszek, J L]] | ||
| + | [[Category: Zhou, P]] | ||
| + | [[Category: Dna damage tolerance]] | ||
| + | [[Category: Replication]] | ||
| + | [[Category: Translesion synthesis]] | ||
Revision as of 05:29, 12 June 2019
Chimeric Pol kappa RIR Rev1 C-terminal domain
| |||||||||||
