Figure 2.
Figure 2. Arginase−ABH complex. a, Omit electron density
map of ABH in the arginase active site averaged over the two
monomers in the asymmetric unit and averaged over the two twin
domains A and B as described in the text. The map is contoured
at 7.7 and
selected active site residues are indicated. Atoms are
color-coded as follows: C = yellow, O = red, N = blue, B = pale
green; water molecules appear as red spheres. This figure was
generated with BOBSCRIPT and Raster3D^34, ^35. b, Summary of
arginase−ABH interactions; manganese coordination interactions
are designated by green dashed lines, and hydrogen bonds are
indicated by black dashed lines. c, Stabilization of the
tetrahedral intermediate (and flanking transition states) in the
arginase mechanism based on the binding mode of ABH.
The above figure is reprinted
by permission from Macmillan Publishers Ltd:
Nat Struct Biol
(1999,
6,
1043-1047)
copyright 1999.
and
selected active site residues are indicated. Atoms are
color-coded as follows: C = yellow, O = red, N = blue, B = pale
green; water molecules appear as red spheres. This figure was
generated with BOBSCRIPT and Raster3D^34, ^35. b, Summary of
arginase−ABH interactions; manganese coordination interactions
are designated by green dashed lines, and hydrogen bonds are
indicated by black dashed lines. c, Stabilization of the
tetrahedral intermediate (and flanking transition states) in the
arginase mechanism based on the binding mode of ABH.