Figure 3.
FIG. 3. Stereo view of the active site and primary
specificity pocket of the thrombin mutant WE. The free form of
WE (red), shown with the 2F[o] - F[c] electron density map
contoured at 0.7 level (orange), is
superimposed to the PPACK-inhibited form (blue). The 215-217
strand in the free form collapses into the primary specificity
pocket and clashes with the Arg residue at the P1 position of
PPACK (green). The r.m.s. deviation between free WE and WE-PPACK
in the 215-221 segment is 2.5 Å. The r.m.s. deviation
between the two monomers in the asymmetric unit of the free WE
structure in the same segment is 0.5 Å. Also notable is
the rotation of the side chain of Asp-189 in the free form that
aligns almost parallel to the backbone as well as the shift in
the side chain of Ser-195 that moves away from its H-bonding
partner His-57.
The above figure is reprinted
by permission from the ASBMB:
J Biol Chem
(2004,
279,
39824-39828)
copyright 2004.
level (orange), is
superimposed to the PPACK-inhibited form (blue). The 215-217
strand in the free form collapses into the primary specificity
pocket and clashes with the Arg residue at the P1 position of
PPACK (green). The r.m.s. deviation between free WE and WE-PPACK
in the 215-221 segment is 2.5 Å. The r.m.s. deviation
between the two monomers in the asymmetric unit of the free WE
structure in the same segment is 0.5 Å. Also notable is
the rotation of the side chain of Asp-189 in the free form that
aligns almost parallel to the backbone as well as the shift in
the side chain of Ser-195 that moves away from its H-bonding
partner His-57.