4EUG
Crystallographic and Enzymatic Studies of an Active Site Variant H187Q of Escherichia Coli Uracil DNA Glycosylase: Crystal Structures of Mutant H187Q and its Uracil Complex
Summary for 4EUG
| Entry DOI | 10.2210/pdb4eug/pdb |
| Related | 2EUG 3EUG 5EUG |
| Descriptor | PROTEIN (GLYCOSYLASE) (2 entities in total) |
| Functional Keywords | glycosylase, hydrolase |
| Biological source | Escherichia coli |
| Cellular location | Cytoplasm: P12295 |
| Total number of polymer chains | 1 |
| Total formula weight | 25696.12 |
| Authors | Xiao, G.,Tordova, M.,Drohat, A.C.,Jagadeesh, J.,Stivers, J.T.,Gilliland, G.L. (deposition date: 1998-12-27, release date: 1999-07-23, Last modification date: 2023-09-13) |
| Primary citation | Drohat, A.C.,Xiao, G.,Tordova, M.,Jagadeesh, J.,Pankiewicz, K.W.,Watanabe, K.A.,Gilliland, G.L.,Stivers, J.T. Heteronuclear NMR and crystallographic studies of wild-type and H187Q Escherichia coli uracil DNA glycosylase: electrophilic catalysis of uracil expulsion by a neutral histidine 187. Biochemistry, 38:11876-11886, 1999 Cited by PubMed: 10508390DOI: 10.1021/bi9910880 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.4 Å) |
Structure validation
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