Figure 4.
Figure 4. Inhibitor binding mode. (a) The molecular surface
of the ST3 active site. The catalytic zinc atom (green) lies on
the surface. The figure was created with GRASP.[46] (b) The
S[1]' pocket is a deep cavity filled by the P[1]' group of the
phosphinic inhibitor RXP03 and two water molecules (blue
spheres). The ST3 surface (in yellow) is coloured in green at
the position of Gln215. The Figure was created with DINO (DINO:
Visualizing Structural Biology developped by Ansgar Philippsen;
http://www.bioz.unibas.ch/ not, vert, similar-xray/dino).
(c) Final 2F[obs] -F[calc] electron density map (white) in the
ST3 active site, contoured at 1.0 sigma. Two of the three His
side-chains ligating the catalytic zinc atom (red sphere) are
represented. The phosphinic inhibitor is coloured in pink. The
Figure was created with Setor.[45]
The above figure is reprinted
by permission from Elsevier:
J Mol Biol
(2001,
307,
577-586)
copyright 2001.
xray/dino).
(c) Final 2F[obs] -F[calc] electron density map (white) in the
ST3 active site, contoured at 1.0 sigma. Two of the three His
side-chains ligating the catalytic zinc atom (red sphere) are
represented. The phosphinic inhibitor is coloured in pink. The
Figure was created with Setor.[45]