4LZB
Uracil binding pocket in Vaccinia virus uracil DNA glycosylase
Summary for 4LZB
| Entry DOI | 10.2210/pdb4lzb/pdb |
| Related | 4DOF |
| Descriptor | Uracil-DNA glycosylase, DIMETHYL SULFOXIDE, POTASSIUM ION, ... (7 entities in total) |
| Functional Keywords | alpha/beta dna glycosylase fold, viral processivity factor, dna binding component, dna repair, a20, hydrolase |
| Biological source | Vaccinia virus (VACV) |
| Total number of polymer chains | 12 |
| Total formula weight | 331044.21 |
| Authors | Schormann, N.,Chattopadhyay, D. (deposition date: 2013-07-31, release date: 2013-12-11, Last modification date: 2023-09-20) |
| Primary citation | Schormann, N.,Banerjee, S.,Ricciardi, R.,Chattopadhyay, D. Structure of the uracil complex of Vaccinia virus uracil DNA glycosylase. Acta Crystallogr.,Sect.F, 69:1328-1334, 2013 Cited by PubMed Abstract: Poxvirus uracil DNA glycosylases are the most diverse members of the family I uracil DNA glycosylases (UNGs). The crystal structure of the uracil complex of Vaccinia virus uracil DNA glycosylase (D4) was determined at 2.03 Å resolution. One uracil molecule was located in the active-site pocket in each of the 12 noncrystallographic symmetry-related D4 subunits. Although the UNGs of the poxviruses (including D4) feature significant differences in the characteristic motifs designated for uracil recognition and in the base-excision mechanism, the architecture of the active-site pocket in D4 is very similar to that in UNGs of other organisms. Overall, the interactions of the bound uracil with the active-site residues are also similar to the interactions previously observed in the structures of human and Escherichia coli UNG. PubMed: 24316823DOI: 10.1107/S1744309113030613 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.03 Å) |
Structure validation
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