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5jkt

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==vaccinia virus D4 P173G mutant /A20(1-50)==
==vaccinia virus D4 P173G mutant /A20(1-50)==
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<StructureSection load='5jkt' size='340' side='right' caption='[[5jkt]], [[Resolution|resolution]] 2.49&Aring;' scene=''>
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<StructureSection load='5jkt' size='340' side='right'caption='[[5jkt]], [[Resolution|resolution]] 2.49&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5jkt]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JKT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JKT FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5jkt]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Vaccinia_virus_Copenhagen Vaccinia virus Copenhagen]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JKT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5JKT FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.49&#8491;</td></tr>
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<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>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<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=5jkt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jkt OCA], [http://pdbe.org/5jkt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jkt RCSB], [http://www.ebi.ac.uk/pdbsum/5jkt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jkt ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5jkt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jkt OCA], [https://pdbe.org/5jkt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5jkt RCSB], [https://www.ebi.ac.uk/pdbsum/5jkt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5jkt ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[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).
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[https://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).
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 5jkt" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 5jkt" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[DNA glycosylase 3D structures|DNA glycosylase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Uracil-DNA glycosylase]]
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[[Category: Large Structures]]
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[[Category: Brazzolotto, X]]
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[[Category: Vaccinia virus Copenhagen]]
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[[Category: Burmeister, W P]]
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[[Category: Brazzolotto X]]
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[[Category: Contesto-Richefeu, C]]
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[[Category: Burmeister WP]]
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[[Category: Iseni, F]]
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[[Category: Contesto-Richefeu C]]
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[[Category: Peyrefitte, C N]]
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[[Category: Iseni F]]
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[[Category: Tarbouriech, N]]
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[[Category: Peyrefitte CN]]
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[[Category: Dna binding]]
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[[Category: Tarbouriech N]]
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[[Category: Dna polymerase binding]]
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[[Category: Dna polymerase processivity factor]]
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[[Category: Hydrolase]]
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[[Category: Hydrolase-replication complex]]
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Current revision

vaccinia virus D4 P173G mutant /A20(1-50)

PDB ID 5jkt

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