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Figure 4.
Figure 4. Displacement of Arg143 in apoSOD^CallA provides a
clue to the structural origin of decreased activity in monomeric
and disulphide-reduced protein. Accompanying the structural
alteration of loop IV, the catalytically important guanidinium
group of R143 moves from its native position and forms new
hydrogen bonds with S59, D52 and the water molecules Wat26 and
Wat68. (a) The 2F[o]–F[c] electron density map of apoSOD^CallA
at 1σ. (b) Schematic representation of the apoSOD^CallA
structure illustrating the hydrogen bonding to R143. (c)
Comparison of the loop IV conformations and positioning of R143
by superposition of the A monomers of apoSOD^CallA (blue) and
holoSOD^CallA (red). Figure 4. Displacement of Arg143 in
apoSOD^CallA provides a clue to the structural origin of
decreased activity in monomeric and disulphide-reduced protein.
Accompanying the structural alteration of loop IV, the
catalytically important guanidinium group of R143 moves from its
native position and forms new hydrogen bonds with S59, D52 and
the water molecules Wat26 and Wat68. (a) The 2F[o]–F[c]
electron density map of apoSOD^CallA at 1σ. (b) Schematic
representation of the apoSOD^CallA structure illustrating the
hydrogen bonding to R143. (c) Comparison of the loop IV
conformations and positioning of R143 by superposition of the A
monomers of apoSOD^CallA (blue) and holoSOD^CallA (red).
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