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4lzb

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==Uracil binding pocket in Vaccinia virus uracil DNA glycosylase==
==Uracil binding pocket in Vaccinia virus uracil DNA glycosylase==
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<StructureSection load='4lzb' size='340' side='right' caption='[[4lzb]], [[Resolution|resolution]] 2.03&Aring;' scene=''>
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<StructureSection load='4lzb' size='340' side='right'caption='[[4lzb]], [[Resolution|resolution]] 2.03&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4lzb]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Vaccinia_virus Vaccinia virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LZB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LZB FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4lzb]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Vaccinia_virus Vaccinia virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LZB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LZB 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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=URA:URACIL'>URA</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]] 2.03&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4dof|4dof]]</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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=URA:URACIL'>URA</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ACAM3000_MVA_101, D4, MVA101R, UNG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10245 Vaccinia virus])</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=4lzb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lzb OCA], [https://pdbe.org/4lzb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lzb RCSB], [https://www.ebi.ac.uk/pdbsum/4lzb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lzb ProSAT]</span></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='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=4lzb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lzb OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4lzb RCSB], [http://www.ebi.ac.uk/pdbsum/4lzb PDBsum]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/UNG_VACCA UNG_VACCA]] 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.
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[https://www.uniprot.org/uniprot/UNG_VACCA UNG_VACCA] 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.
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
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<div class="pdbe-citations 4lzb" style="background-color:#fffaf0;"></div>
==See Also==
==See Also==
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*[[Uracil-DNA glycosylase|Uracil-DNA glycosylase]]
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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]]
[[Category: Vaccinia virus]]
[[Category: Vaccinia virus]]
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[[Category: Chattopadhyay, D]]
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[[Category: Chattopadhyay D]]
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[[Category: Schormann, N]]
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[[Category: Schormann N]]
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[[Category: A20]]
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[[Category: Alpha/beta dna glycosylase fold]]
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[[Category: Dna binding component]]
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[[Category: Dna repair]]
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[[Category: Hydrolase]]
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[[Category: Viral processivity factor]]
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Current revision

Uracil binding pocket in Vaccinia virus uracil DNA glycosylase

PDB ID 4lzb

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