Figure 2 - full size

 

Figure 2.
FIGURE 2. A, superimposition of the three-dimensional structures of SmCypA^red (blue ribbon) and SmCypA^ox (magenta), highlighting the N and C termini. B, detailed view of the substrate/inhibitor binding site of SmCypA^red (the view is 180° rotated with respect to panel A). Cys-122, Cys-126, and residues forming the pockets listed in Table 2 are shown in ball-and-stick format. The red circles indicate the approximate location of pockets 1, 2, and 3. C, as in B, shown is the substrate/inhibitor binding site of SmCypA^ox, containing the disulfide bond. D, magnified view of the active site loop. The interactions of water molecule (W40) with the sulfur atoms of Cys-122 and Cys-126 are shown together with their distances from the carbonyl groups of the loop, which make contact with the water. This figure was generated using PyMOL (34).

The above figure is reprinted by permission from the ASBMB: J Biol Chem (2007, 282, 24851-24857) copyright 2007.