Figure 5

Substrate binding pockets of (HUMAN)NAT2*4, (MOUSE)NAT2_F125S, (MOUSE)NAT2_R127G and (MOUSE)NAT2_R127L with POA docked. Maximised view of the active sites of (A): (HUMAN)NAT2*4; (B): (MOUSE)NAT2_F125S; (C): (MOUSE)NAT2_R127G; (D): (MOUSE)NAT2_R127L with the arylamine substrate POA docked. The overall structure of each NAT enzyme is drawn as a ribbon diagram: (HUMAN)NAT2*4 is coloured in mauve [PDB:2PFR] [9] and (MOUSE)NAT2 mutants in light blue. The side chains of the key residues involved in substrate binding within the active site are drawn in stick representation and labelled with carbon atoms in the corresponding colour of the enzyme, nitrogen in blue, oxygen in red and sulphur in yellow. The arylamine substrate POA is labelled with carbon atoms in orange, nitrogen in blue, oxygen in red and polar hydrogen in gray. The figures were generated using PyMOL [41].