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Fig. 2 | Journal of Cheminformatics

Fig. 2

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

Fig. 2

a Percentage of cofactor and SAM-competitive inhibitors that interact with a given PLIF interacting residue according to interaction type. b Summary of detected HB interactions for SAM. Circles represent PLIF interacting residues: numbers correspond to residue alignment position (conserved residues are shown, if applicable) and (numbers) correspond to the number of different PKMTs for which this interaction was detected. Red, blue and orange colors are for backbone, side chain or both types of HB contacts, respectively. The network of six HBs described by Campagna-Slater et al. [19] is labeled with stars: (1) N7 of SAM as HBA with the highly conserved His (Cys in PRDM9) of the NHS/CxxPN motif (position 1362); (2) amine group of the adenine ring with this same residue; amine group of the methionine fragment acting as HBD (3) with the Asn (1361) of the NHS/CxxPN motif and (4) the x residue at position 557 of the conserved motif GxG and (5) the residue upstream of the GxG motif (545); (6) the carboxylate group of the methionine moiety acting as HBA with the x residue of the GxG motif (557)

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