Figure 4.
Figure 4 Stereoviews of inhibitors (2), (3) and (4) at the
enzyme active site. Unbiased F[obs] - F[calc] electron-density
maps showing the inhibitors and metal ions are contoured at 3
.
(a) The MnII-form selective inhibitor (2) with the MnII-form
enzyme. (b) The MnII-form selective inhibitor (3) with the
MnII-form enzyme. (c) The CoII-form selective inhibitor (4) with
the CoII-form enzyme. For clarity, only the five conserved
residues forming the common dinuclear metal site (Asp97, Asp108,
His171, Glu204 and Glu235) plus His79 and His178 are shown.
Protein residues are colored grey for carbon, red for oxygen and
blue for nitrogen. Inhibitors are colored the same way, except
that carbons are yellow, sulfurs orange, chlorines green and
fluorines cyan. MnII ions are shown as green spheres, while CoII
ions are shown as magenta spheres. Water molecules are shown as
smaller red spheres. Hydrogen bonds and metal interactions are
shown as black dashed lines.
The above figure is reprinted
by permission from the IUCr:
Acta Crystallogr D Biol Crystallogr
(2006,
62,
425-432)
copyright 2006.
.
(a) The MnII-form selective inhibitor (2) with the MnII-form
enzyme. (b) The MnII-form selective inhibitor (3) with the
MnII-form enzyme. (c) The CoII-form selective inhibitor (4) with
the CoII-form enzyme. For clarity, only the five conserved
residues forming the common dinuclear metal site (Asp97, Asp108,
His171, Glu204 and Glu235) plus His79 and His178 are shown.
Protein residues are colored grey for carbon, red for oxygen and
blue for nitrogen. Inhibitors are colored the same way, except
that carbons are yellow, sulfurs orange, chlorines green and
fluorines cyan. MnII ions are shown as green spheres, while CoII
ions are shown as magenta spheres. Water molecules are shown as
smaller red spheres. Hydrogen bonds and metal interactions are
shown as black dashed lines.