On the base of the channel is the methyltransfer pore, which connects the pocket to the AdoMet-binding cleft. In each proteins, the partitions of the lysine-binding channel are formed by hydrophobic residues that have interaction in van der Waals interactions with the lysine side chain (Determine 4b,c ). Min J, Zhang X, Cheng X, Grewal SI, Xu RM: Structure of the SET area histone lysine methyltransferase Clr4.

A protein sequence alignment of the SET domains of several consultant histone lysine methyltransferases (HKMT) grouped based on their histone-lysine specificity. Methylation of particular histone lysine residues serves as a publish-translational epigenetic modification that controls the expression of genes by serving as 'markers' for the recruitment of specific complexes that direct the group of chromatin. Lysine helps forestall the herpes virus from rising.

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