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This pore is rimmed with several structurally conserved carbonyl oxygens in addition to the hydroxyl group of the invariant tyrosine from the carboxyl terminus of the SET domain (Figure 1 ). These carbonyl and [hydroxyl oxygens](http://gitlab.tangguo.ren/kassie58163335/3228381/issues/2) have been proposed to facilitate the transfer of the methyl group during catalysis 16 , 21 , 24 As well as, tyrosine residues within the lysine-binding clefts of SET7/9 (Tyr245 and Tyr305) and [solicitor law firm](https://firstlikecab.com/index.php/2017/02/01/we-have-taken-delivery-of-our-new-fleet-2/) DIM-5 (Tyr178) hydrogen-bond to the lysine ε-amino group, aligning it for a methyltransfer with AdoMet (Determine 4b,c ). Mutation of Tyr245 or Tyr305 in SET7/9 (Figure 4b ) alters its specificity from an H3 K4 mono-methylase to a tri- and di-methylase, respectively 16 , 21 , whereas an Phe281Tyr mutation in the lysine-binding pocket of DIM-5 (Determine 4c ) converts this protein to an H3 K9 mono- or di-methylase 16 These mutations exemplify the F/Y switch (Figure 1 ) that establishes SET-area product specificities.
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