2.1.1.184	2-([[(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)methyl][3-(1H-imidazol-1-yl)propyl]amino]methyl)-1H-isoindole-1,3(2H)-dione	i.e. PD00556	74055	
2.1.1.184	4-methyl-2,6-di[(4-methylphenyl)thio]nicotinonitrile	i.e. RF00667	74053	
2.1.1.184	additional information	the crystal structure of ErmC’ methyltransferase is used as a target for structure-based virtual screening of a database composed of 58679 lead-like compounds. Among 77 compounds selected for experimental validation (63 predicted to bind to the catalytic pocket and 14 compounds predicted to bind to the putative RNA binding site), several novel inhibitors are found that decrease the minimal inhibitory concentration of a macrolide antibiotic erythromycin toward an Escherichia coli strain that constitutively expresses ErmC'. Analysis of docking models of the identified inhibitors suggests a novel strategy to develop potent and clinically useful inhibitors	2	
2.1.1.184	N6-dimethyladenine2085 containing 23S rRNA	linear competitive inhibition kinetics with RNA as the variable substrate, mixed inhibition with S-adenosyl-L-methionine as the variable substrate	39753	
2.1.1.184	nicotinaldehyde-N-[3-(2-chlorobenzyl)-3H-[1,2,3]triazolo[4,5-d]pyrimidin-7-yl]hydrazone	i.e. HTS12610	74054	
2.1.1.184	S-adenosyl-L-homocysteine	linear competitive pattern with S-adenosyl-L-methionine as the variable substrate, and a mixed inhibition kinetics with RNA	36	
2.1.1.184	S-adenosyl-L-homocysteine	-	36	
2.1.1.184	sinefungin	competitive	659