Figure 4.
Fig. 4. Environment of the redox active site. a, Prx-Grx
interaction and glutathione binding in the hyPrx5 tetramer.
Glutathione model (shown in the figure as a ball and stick
diagram) was created by superposing the complex structure of
Grx3-glutathione (PDB code 3GRX) on the hyPrx5 Grx domain.
Surfaces of Prx (monomer A) and Grx (monomer D) domains are
colored red and gold, respectively. Redox active cysteines
(Cys-49 and Cys-180) and residues involved in the Prx-Grx
interaction are labeled. b, stereo view of the 2F[o] F[c]
electron density map. The electron density map around the Prx
active site of hyPrx5 is presented as superimposed with the
refined model. The map was contoured at a 0.9 level. c,
stereo view of the Prx active site of hyPrx5. The side chains of
residues (Arg-126 and Thr-46) contributing to the reactivity of
the sulfur atom of Cys-49 were drawn as a ball-and-stick
representation. Distances between the interacting atoms are
shown in the figure.
The above figure is reprinted
by permission from the ASBMB:
J Biol Chem
(2003,
278,
10790-10798)
copyright 2003.
F[c]
electron density map. The electron density map around the Prx
active site of hyPrx5 is presented as superimposed with the
refined model. The map was contoured at a 0.9 
level. c,
stereo view of the Prx active site of hyPrx5. The side chains of
residues (Arg-126 and Thr-46) contributing to the reactivity of
the sulfur atom of Cys-49 were drawn as a ball-and-stick
representation. Distances between the interacting atoms are
shown in the figure.