2.1.1.202	additional information	the S-adenosyl-L-methionine analigue sinefungin is bound in a negatively charged pocket near helix alpha8, binding structure, detailed overview	719968	
2.1.1.202	S-adenosyl-L-methionine	-	735680, 735864, 735907, 736856, 737227, 756866, 757702, 757846, 757867, 758103, 758477	
2.1.1.202	S-adenosyl-L-methionine	cofactor interacting residues in hNSun6 are mainly composed of conserved residues Leu241, Cys242, Pro325 and Leu354. In addition, the side chain of residue Asp293 recognizes the N6 of the adenine ring. Asp293 is conserved as Asp or Glu in the RNA:m5C MTase family	757846	
2.1.1.202	S-adenosyl-L-methionine	helix alpha8 can adopt two different conformations, thereby controlling the entry of S-adenosyl-L-methionine into the active site	719968