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Figure 3.
Figure 3. Detailed Structural Analysis of SANOS(A) Stereo
diagram showing the dimer interface of SANOS. The main chains
are shown as ribbons and coils, with the A chain colored green
and the B chain colored blue. The side chains of key residues
involved in the interface interactions are shown as balls and
sticks and colored orange and cyan for the A and B chains,
respectively. The yellow dashed lines represent the hydrogen
bonds between the two chains. The four segments from each chain
are labeled I-IV (residues 233-240, 259-280, 288-291, and
314-330, respectively).(B) Electrostatic surface (A chain) and
ribbons (B chain) showing the charge distribution on the
molecular surface and the dimer interface. The positively and
negatively charged areas are colored blue and red, respectively.
All ligands for both monomers are shown as dark yellow-colored
space-filling representations. The side chains that are only
conserved among bacterial NOSs are shown as balls and sticks,
with the nitrogen and oxygen atoms colored in blue and red,
respectively.(C) Stereo view of one set of ligand binding sites
of SANOS. The main chain backbone of the A and B chains are
colored dark and light gray, respectively. Haem, SEITU, and the
nicotinamide and ribose moieties of NAD^+ are colored by atoms,
with carbon atoms in dark gray. The haem iron is shown as a
magenta sphere. The side chains of key residues are drawn as
ball-and-stick representations and colored by atoms, with their
carbon atoms in cyan. Water molecules are represented as red
spheres. The broken yellow lines indicate hydrogen bonds between
the substrates and the protein. SEITU, H[4]B, and a section of
the hook from bovine eNOS that interacts with the pterin
(colored orange) have been overlaid onto the SANOS interface
ligand binding site.
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