5jx3
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Wild type D4 in orthorhombic space group== | |
| - | + | <StructureSection load='5jx3' size='340' side='right' caption='[[5jx3]], [[Resolution|resolution]] 2.30Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[5jx3]] is a 8 chain structure. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2owr 2owr]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JX3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JX3 FirstGlance]. <br> | |
| - | + | </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=GOL:GLYCEROL'>GOL</scene></td></tr> | |
| - | [[Category: | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5jx0|5jx0]], [[5jx8|5jx8]]</td></tr> |
| + | <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> | ||
| + | <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=5jx3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jx3 OCA], [http://pdbe.org/5jx3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jx3 RCSB], [http://www.ebi.ac.uk/pdbsum/5jx3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jx3 ProSAT]</span></td></tr> | ||
| + | </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: Chattopadhyay, D]] | [[Category: Chattopadhyay, D]] | ||
[[Category: Schormann, N]] | [[Category: Schormann, N]] | ||
| + | [[Category: Dna repair enzyme component of processivity factor poxvirus]] | ||
| + | [[Category: Hydrolase]] | ||
Revision as of 02:12, 13 July 2016
Wild type D4 in orthorhombic space group
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