Figure 3 - full size

 

Figure 3.
Fig. 3. Structure alignment of N-CaM with N-terminal domain of the NMR structure of apo-CaM (left, 1CFD) and the X-ray structure of Ca^2+-CaM (right, 1CLL). The residues involved in ion coordination are shown as sticks and labeled. These global alignments were performed using helices A and D, and show that our structure is predominantly in the closed conformation. 1CFD and 1CLL are presented as transparent. The two helix–loop–helix EF-hand Zn^2+-binding sites are shown in different colors: EF-hand I (helices A and B), rose red; EF-hand II (helices C and D), lime green. The spheres show the two Zn^2+ ions present in these binding sites. The zinc ion in site 2 has double occupancy. There is also a cacodylate molecule present from the crystal growth buffer with arsenic shown in purple.

The above figure is reprinted by permission from Elsevier: J Mol Biol (2007, 374, 517-527) copyright 2007.