Skip to main content


Fig. 7 | Journal of Cheminformatics

Fig. 7

From: Novel pharmacological maps of protein lysine methyltransferases: key for target deorphanization

Fig. 7

a Percentage of substrate-competitive inhibitors that interact with a given PLIF interacting residue according to interaction type. b–h Mapping of PLIF interacting residues for each of the seven PKMTs. Red balls correspond to residues for which at least one interaction was detected for all ligands (in orange) of this protein and grey balls to any of the remaining 24 different PLIF interacting residues (if conserved for the given PKMT at the corresponding positioning of the alignment) and for which no interaction was detected for any of the ligands of this PKMT. Note that because of structural protein differences in the alignment not all PLIF interacting residues could be mapped onto each protein. For reference, SAH is shown in blue

Back to article page