Figure 1.
Figure 1 Crystal structure of the human thrombin–haemadin
complex. (A) Structure of the crystallographic trimer present in
the asymmetric unit. Monomers are labelled A, B and C. Thrombin
molecules are shown as red, yellow and green ribbons; the C[
]traces
of the three inhibitors are presented as colour-coded van der
Waals spheres (red, oxygen; blue, nitrogen; grey, carbon). (B)
Stereo diagram of complex molecule A. The protease is shown in
its 'standard orientation' (Bode et al., 1992), i.e. with the
active-site cleft facing the viewer and substrates running from
left to right. Side chains of the catalytic triad residues are
shown explicitly, as well as the side chains of the interacting
residues Asp189 (thrombin) and Arg2I (haemadin) (colour coded as
in Figure 1A). Also shown (unlabelled) are the side chains of
the basic residues of the heparin-binding site (thrombin), as
well as the side chains of the acidic residues of haemadin's
C-terminal tail. This figure and Figures 3, 5A, 7A and 8 were
prepared with SETOR (Evans, 1993).
The above figure is reprinted
from an Open Access publication published by Macmillan Publishers Ltd:
EMBO J
(2000,
19,
5650-5660)
copyright 2000.
]traces
of the three inhibitors are presented as colour-coded van der
Waals spheres (red, oxygen; blue, nitrogen; grey, carbon). (B)
Stereo diagram of complex molecule A. The protease is shown in
its 'standard orientation' (Bode et al., 1992), i.e. with the
active-site cleft facing the viewer and substrates running from
left to right. Side chains of the catalytic triad residues are
shown explicitly, as well as the side chains of the interacting
residues Asp189 (thrombin) and Arg2I (haemadin) (colour coded as
in Figure 1A). Also shown (unlabelled) are the side chains of
the basic residues of the heparin-binding site (thrombin), as
well as the side chains of the acidic residues of haemadin's
C-terminal tail. This figure and Figures 3, 5A, 7A and 8 were
prepared with SETOR (Evans, 1993).