Figure 5.
Figure 5. Standard view from the Pl
substrate towards the active site of the Pl
enzyme in complex with SAK (shown as a solid surface).
Coloring of the Pl
enzyme is made according to the electrostatic potential. a,
Intact Pg activation loop (Lys 10(557)−Val 21(567)) as modeled
on residues Lys 10(557) and Cys 20(566) of the cleaved substrate
and on the tripeptidyl moiety bound to the Pl
enzyme. b, Cleaved Pg activation loop as seen in the crystal
structure. Only the N- and the C-terminal ends of the cleaved
Pl
substrate (Lys 10(557)−Gly 14(560) and Val 16(562)-Val
21(567)) are shown. Figure produced with GRASP^30.
The above figure is reprinted
by permission from Macmillan Publishers Ltd:
Nat Struct Biol
(1998,
5,
917-923)
copyright 1998.
Pl
substrate towards the active site of the 
Pl
enzyme is made according to the electrostatic potential. a,
Intact Pg activation loop (Lys 10(557)−Val 21(567)) as modeled
on residues Lys 10(557) and Cys 20(566) of the cleaved substrate
and on the tripeptidyl moiety bound to the