Figure 1.
FIGURE 1. Overlay of the ribbon plots of the structures of
the thrombin mutant C191A/C220A in the free (wheat) and
PPACK-inhibited (cyan) forms. The r.m.s.d. between the two
structures is 0.42 Å. Structures are displayed in the
standard Bode orientation (3) with the active site in the
middle. The catalytic residues His-57, Asp-102, and Ser-195 are
rendered as sticks as is Asp-189 in the primary specificity
pocket and the inhibitor PPACK (green). Relevant regions of the
enzyme are noted. The C atoms of Ala-191 and
Ala-220 at the sites of mutation are indicated by arrows (black
for Ala-220, red for Ala-191). Note the autolysis loop that is
completely ordered only in the PPACK-bound form.
The above figure is reprinted
by permission from the ASBMB:
J Biol Chem
(2007,
282,
27165-27170)
copyright 2007.
atoms of Ala-191 and
Ala-220 at the sites of mutation are indicated by arrows (black
for Ala-220, red for Ala-191). Note the autolysis loop that is
completely ordered only in the PPACK-bound form.