Figure 4.
Figure 4. Stereo section of the final 2.65 Å 2F[obs] - F[
calc] electron density map (blue) contoured at 1 around
the interface between Pl
enzyme (green carbons) and SAK (yellow carbons). The view is
similar to the standard orientation shown in Figs 2 and 5. Side
chains from both molecules form an extended network of salt
bridges and charged hydrogen bonds. The strong Arg
175(719)−Glu 46SAK salt bridge is buried from the solvent by
Tyr 44SAK. Furthermore, Arg 43SAK and Tyr 44SAK protrude into
the active site of Pl,
providing more narrow subsite boundaries. Figure produced with
SETOR^28.
The above figure is reprinted
by permission from Macmillan Publishers Ltd:
Nat Struct Biol
(1998,
5,
917-923)
copyright 1998.
around
the interface between 
Pl
enzyme (green carbons) and SAK (yellow carbons). The view is
similar to the standard orientation shown in Figs 2 and 5. Side
chains from both molecules form an extended network of salt
bridges and charged hydrogen bonds. The strong Arg
175(719)−Glu 46SAK salt bridge is buried from the solvent by
Tyr 44SAK. Furthermore, Arg 43SAK and Tyr 44SAK protrude into
the active site of 
Pl,
providing more narrow subsite boundaries. Figure produced with
SETOR^28.