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5jkr
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==vaccinia virus D4/A20(1-50)w43a mutant== | |
| - | + | <StructureSection load='5jkr' size='340' side='right' caption='[[5jkr]], [[Resolution|resolution]] 2.60Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[5jkr]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JKR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JKR FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | |
| - | [[Category: | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Uracil-DNA_glycosylase Uracil-DNA glycosylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.2.27 3.2.2.27] </span></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=5jkr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jkr OCA], [http://pdbe.org/5jkr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jkr RCSB], [http://www.ebi.ac.uk/pdbsum/5jkr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jkr ProSAT]</span></td></tr> |
| - | [[Category: | + | </table> |
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/UNG_VACCC UNG_VACCC]] Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine. Also part of a heterodimeric processivity factor which potentiates the DNA polymerase activity. Binds to DNA (By similarity). [[http://www.uniprot.org/uniprot/A20_VACCC A20_VACCC]] Plays an essential role in viral DNA replication by acting as the polymerase processivity factor together with protein D4. May serve as a bridge which links the DNA polymerase E9 and the uracil DNA glycosylase (By similarity). | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Uracil-DNA glycosylase]] | ||
| + | [[Category: Brazzolotto, X]] | ||
| + | [[Category: Burmeister, W P]] | ||
[[Category: Contesto-Richefeu, C]] | [[Category: Contesto-Richefeu, C]] | ||
[[Category: Iseni, F]] | [[Category: Iseni, F]] | ||
| - | [[Category: | + | [[Category: Peyrefitte, C N]] |
[[Category: Tarbouriech, N]] | [[Category: Tarbouriech, N]] | ||
| + | [[Category: Dna binding]] | ||
| + | [[Category: Dna polymerase binding]] | ||
| + | [[Category: Dna polymerase processivity factor]] | ||
| + | [[Category: Hydrolase-replication complex]] | ||
Revision as of 15:32, 14 September 2016
vaccinia virus D4/A20(1-50)w43a mutant
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