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Figure 4.
Figure 4. Substrate binding in UMPK. (a) Stereo view of the
C^α trace of the substrate-binding sites, with bound
Mg[2]AMPPNP and UMP coloured. Amino acid side-chains are also in
colour, in thinner trace. (b) Stereoscopic detailed
representation of the phosphoryl group transfer site in the
complex with Mg[2]AMPPNP and UMP. Mg ions and water molecules
are drawn as purple and cyan spheres, respectively. Nearby
protein residues are shown in thinner trace. Hydrogen bonds and
coordination bonds with Mg are shown as red lines, indicating
the interatomic distances (in Å). The interatomic distance
between the attacking O atom of UMP and the γ-P atom is
represented with a blue line. (c) and (d) Plots of the
interactions between the protein and (c) UMP or (d) Mg[2]AMPPNP
in the ternary complex. The letter W denotes a water molecule.
Distances are in Å. Figure 4. Substrate binding in
UMPK. (a) Stereo view of the C^α trace of the substrate-binding
sites, with bound Mg[2]AMPPNP and UMP coloured. Amino acid
side-chains are also in colour, in thinner trace. (b)
Stereoscopic detailed representation of the phosphoryl group
transfer site in the complex with Mg[2]AMPPNP and UMP. Mg ions
and water molecules are drawn as purple and cyan spheres,
respectively. Nearby protein residues are shown in thinner
trace. Hydrogen bonds and coordination bonds with Mg are shown
as red lines, indicating the interatomic distances (in Å).
The interatomic distance between the attacking O atom of UMP and
the γ-P atom is represented with a blue line. (c) and (d) Plots
of the interactions between the protein and (c) UMP or (d)
Mg[2]AMPPNP in the ternary complex. The letter W denotes a water
molecule. Distances are in Å. Parts (c) and (d) were drawn
with LIGPLOT.[3]^50
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