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. Author manuscript; available in PMC: 2019 Jun 11.
Published in final edited form as: Biochemistry. 2017 Jul 20;56(30):3934–3944. doi: 10.1021/acs.biochem.7b00476

Figure 6. 1,6-DDMT-binding site of BthII1283.

Figure 6.

Stereoview ( left) and schematic (right) representations of interactions of 1,6-DDMT with residues of the Class I methyltransferase fold (light blue), N-teminal extension (salmon), first internal extension (light green), and second internal extension (light purple) in (A) monomer A and (B) monomer B of the asymmetric unit. SAH and 1,6-DDMT are shown as balls and sticks. Dashed lines represent potential hydrogen bonds. Water molecules are shown as red spheres in the stereo diagrams and ‘W’ in the schematic drawings. The side chain of Trp47 stacks against the azapteridine ring system of 1,6-DDMT but is omitted for clarity.