Fig. 2.
Overall structure of hMAO A. The orientation is as in Fig. 1. (A) Ribbon representation of the monomer. The FAD-binding domain (residues 13–88, 220–294, and 400–462) is in blue; the substrate-binding domain (89–219 and 295–399) is in red; and the C-terminal membrane region (463–506) is in green. Residues 1–12, 111–115, and 507–527 are not visible in the electron density map. A dashed line connects residues 110–116. FAD and clorgyline are depicted in yellow and cyan ball-and-stick representation, respectively. The active site cavity-shaping loop 210–216 is depicted as black coil. (B) Stereoview of the superposition of the Cα traces of human MAO A (black) and MAO B (red). FAD and clorgyline bound to MAO A are shown as black ball-and-stick. Loop 210–216 of hMAO A and the equivalent loop 201–206 of hMAO B are shown as thick coils to highlight their different conformations.