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SAM-dependent methyltransferase
This family contains a SAM (S-adenosyl methyltransferase) domain, with a central beta sheet with 3 alpha-helices on both sides. Crystal packing analysis of the structure PDB:3giw from Swiss:Q82L35 suggests that a monomer is the solution state oligomeric form. An unidentified ligand (UNL, cyan) was found at the putative active site surrounded by the residues His57, His170, Phe171, Tyr216 and Met22 . The UNL is likely to be a phenylalanine or phenylalanine-like molecule. (details derived from TOPSAN). [1]. 18154359. The histamine N-methyltransferase T105I polymorphism affects active site structure and dynamics. Rutherford K, Parson WW, Daggett V;. Biochemistry. 2008;47:893-901. (from Pfam)
class I SAM-dependent methyltransferase that uses S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy)
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