Figure 6.
Figure 6. Fig 6 a, The coordination geometry of the zinc binding
site at the dimer interface. The zinc ion is represented by a
green sphere and waters by red spheres. The structural elements
in the two monomers are colored in brown and blue respectively.
The C-terminal end of helix 1
is distorted by forming a 3[10]-helix. The coordination angles
subtended by the zinc and ligated atoms are in the range of
99−117°. b, Ribbon diagram of the pf PDO dimer. The two
monomers are colored in brown and blue respectively. The active
site disulfides are shown in ball-and-stick representation and
colored in yellow. The two zinc ions, which are related by the
crystallographic two-fold axis, are shown by green spheres.
The above figure is reprinted
by permission from Macmillan Publishers Ltd:
Nat Struct Biol
(1998,
5,
602-611)
copyright 1998.
1
is distorted by forming a 3[10]-helix. The coordination angles
subtended by the zinc and ligated atoms are in the range of
99−117°. b, Ribbon diagram of the pf PDO dimer. The two
monomers are colored in brown and blue respectively. The active
site disulfides are shown in ball-and-stick representation and
colored in yellow. The two zinc ions, which are related by the
crystallographic two-fold axis, are shown by green spheres.