Figure 2.
FIG. 2. Overall structure of the Pim-1·staurosporine
complex. The structure is shown with -sheets as arrows and
the -helices as cylinders.
The N-terminal domain (dark blue) is shown with the glycine-rich
loop drawn in green. The hinge connecting the two domains is
colored orange. The C-terminal domain is shown in light blue
with the activation loop shown in yellow. Staurosporine (red) is
shown in the active site, bound between the Phe^49 side chain
(colored gray in the glycine-rich loop) and the hinge region.
The salt bridge stabilizing the conformation of the activation
loop is formed by residues Asp200 and Arg166 side chains, drawn
with gray carbon atoms. The site of phosphorylation, Ser261, is
shown. All of the structural figures were prepared with Pymol
(54).
The above figure is reprinted
by permission from the ASBMB:
J Biol Chem
(2005,
280,
13728-13734)
copyright 2005.
-sheets as arrows and
the 
-helices as cylinders.
The N-terminal domain (dark blue) is shown with the glycine-rich
loop drawn in green. The hinge connecting the two domains is
colored orange. The C-terminal domain is shown in light blue
with the activation loop shown in yellow. Staurosporine (red) is
shown in the active site, bound between the Phe^49 side chain
(colored gray in the glycine-rich loop) and the hinge region.
The salt bridge stabilizing the conformation of the activation
loop is formed by residues Asp200 and Arg166 side chains, drawn
with gray carbon atoms. The site of phosphorylation, Ser261, is
shown. All of the structural figures were prepared with Pymol
(54).