4qcb: Difference between revisions

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'''Unreleased structure'''
==Protein-DNA complex of Vaccinia virus D4 with double-stranded non-specific DNA==
 
<StructureSection load='4qcb' size='340' side='right' caption='[[4qcb]], [[Resolution|resolution]] 2.89&Aring;' scene=''>
The entry 4qcb is ON HOLD  until Nov 11 2016
== Structural highlights ==
 
<table><tr><td colspan='2'>[[4qcb]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QCB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QCB FirstGlance]. <br>
Authors: Schormann, N., Banerjee, S., Ricciardi, R., Chattopadhyay, D.
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
 
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4dof|4dof]], [[4dog|4dog]], [[4lzb|4lzb]], [[4qc9|4qc9]], [[4qca|4qca]]</td></tr>
Description: Protein-DNA complex of Vaccinia virus D4 with double-stranded non-specific DNA
<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: Unreleased Structures]]
<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=4qcb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qcb OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4qcb RCSB], [http://www.ebi.ac.uk/pdbsum/4qcb PDBsum]</span></td></tr>
[[Category: Schormann, N]]
</table>
== Function ==
[[http://www.uniprot.org/uniprot/UNG_VACCW UNG_VACCW]] 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).
__TOC__
</StructureSection>
[[Category: Uracil-DNA glycosylase]]
[[Category: Banerjee, S]]
[[Category: Banerjee, S]]
[[Category: Chattopadhyay, D]]
[[Category: Ricciardi, R]]
[[Category: Ricciardi, R]]
[[Category: Chattopadhyay, D]]
[[Category: Schormann, N]]
[[Category: A20]]
[[Category: Component of processivity factor]]
[[Category: Dna repair enzyme]]
[[Category: Hydrolase-dna complex]]
[[Category: Poxvirus]]