Fig. 3
From: Novel pharmacological maps of protein lysine methyltransferases: key for target deorphanization
Mapping of PLIF interacting residues for 4 complexes of representative PKMTs complexed with either SAM or SAH. a KMT5A (PDB: 4IJ8; SAM); b EZH2 (PDB: 5HYN; SAH); c PRDM9 (PDB: 4C1Q; SAH) and d KMT5B (PDB: 5WBV; SAM). All 30 PLIF interacting residues for SAM-competitive inhibitors are shown, considering that the residue can be mapped in the alignment. Balls correspond to either backbone (red) or side chain (green) atoms establishing HB contacts or hydrophobic contacts (blue), respectively. Grey balls, marked at the Cα atom, correspond to PLIF interacting residues for which the corresponding ligand does not establish any interaction