1Q65
CRYSTAL STRUCTURE OF TGT IN COMPLEX WITH 2,6-DIAMINO-8-(2-dimethylaminoethylsulfanylmethyl)-3H-QUINAZOLIN-4-ONE crystallized at pH 5.5
Summary for 1Q65
| Entry DOI | 10.2210/pdb1q65/pdb |
| Related | 1Q4W 1Q63 1Q66 1pud |
| Descriptor | Queuine tRNA-ribosyltransferase, ZINC ION, 2,6-DIAMINO-8-(2-DIMETHYLAMINOETHYLSULFANYLMETHYL)-3H-QUINAZOLIN-4-ONE, ... (4 entities in total) |
| Functional Keywords | transferase |
| Biological source | Zymomonas mobilis |
| Total number of polymer chains | 1 |
| Total formula weight | 43284.50 |
| Authors | Brenk, R.,Meyer, E.,Reuter, K.,Stubbs, M.T.,Garcia, G.A.,Klebe, G. (deposition date: 2003-08-12, release date: 2004-04-13, Last modification date: 2023-08-16) |
| Primary citation | Brenk, R.,Meyer, E.,Reuter, K.,Stubbs, M.T.,Garcia, G.A.,Diederich, F.,Klebe, G. Crystallographic Study of Inhibitors of tRNA-guanine Transglycosylase Suggests a New Structure-based Pharmacophore for Virtual Screening. J.Mol.Biol., 338:55-75, 2004 Cited by PubMed Abstract: The enzyme tRNA-guanine transglycosylase (TGT) is involved in the pathogenicity of Shigellae. As the crystal structure of this protein is known, it is a putative target for the structure-based design of inhibitors. Here we report a crystallographic study of several new ligands exhibiting a 2,6-diamino-3H-quinazolin-4-one scaffold, which has been shown recently to be a promising template for TGT-inhibitors. Crystal structure analysis of these complexes has revealed an unexpected movement of the side-chain of Asp102. A detailed analysis of the water network disrupted by this rotation has lead to the derivation of a new composite pharmacophore. A virtual screening has been performed based on this pharmacophore hypothesis and several new inhibitors of micromolar binding affinity with new skeletons have been discovered. PubMed: 15050823DOI: 10.1016/j.jmb.2004.02.019 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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