EC Number   |
Reference |
|---|
   2.1.1.184 | crystallized by the hanging drop vapor diffusion method. Structure of the apo-enzyme at 2.2 A resolution. The crystal structures of ErmC' and of its complexes with the cofactor S-adenosyl-L-methionine, the reaction product S-adenosyl-L-homocysteine and the methyltransferase inhibitor sinefungin, respectively, show that the enzyme undergoes small conformational changes upon ligand binding |
705109 |
| 2.1.1.184 | crystals of ErmC' are obtained by the hanging-drop vapor diffusion method. Crystal structure of ErmC' (a naturally occurring variant of ErmC) determined at 3.0 A resolution by multiple anomalous diffraction phasing methods. The structure consists of a conserved alpha/beta amino-terminal domain which binds the cofactor S-adenosyl-L-methionine, followed by a smaller, alpha-helical RNA-recognition domain |
485441 |
| 2.1.1.184 | the crystal structure of ErmCΒ methyltransferase is used as a target for structure-based virtual screening of a database composed of 58679 lead-like compounds. Analysis of docking models of the identified inhibitors suggests a novel strategy to develop potent and clinically useful inhibitors |
703219 |
