Figure 2.
Fig. 2. The InsP[6]-binding and active sites. (A) Electrostatic
surface potential of the CPD as viewed from above the
InsP[6]-binding site. Blue denotes a positively charged surface;
red denotes a negatively charged surface. InsP[6] is shown in
the binding site as a stick model. (B) Close-up view of the
InsP[6]-binding site. Side chains that directly interact with
InsP[6] are labeled and shown as yellow sticks. The electron
density for InsP[6] (2F[obs] – F[calc]) is contoured at 2 .
(C) Surface topology of the CPD active site. The P1 substrate
pocket, C140, and H91 are highlighted in orange, yellow, and
blue, respectively. The N terminus is shown as a yellow ribbon,
terminating at Ile5 and highlighting the threading of this
region along the surface of the core domain. The remaining
residues not visible at the N terminus are depicted as a yellow
dashed line to illustrate the approximate positioning of the
chain during catalysis. (D) Close-up view of the P1 substrate
pocket. Amino acids that line the pocket are labeled and colored
orange. InsP[6] is shown as in (B) to demonstrate the position
of the catalytic site with respect to the InsP[6]-binding site.
.
(C) Surface topology of the CPD active site. The P1 substrate
pocket, C140, and H91 are highlighted in orange, yellow, and
blue, respectively. The N terminus is shown as a yellow ribbon,
terminating at Ile5 and highlighting the threading of this
region along the surface of the core domain. The remaining
residues not visible at the N terminus are depicted as a yellow
dashed line to illustrate the approximate positioning of the
chain during catalysis. (D) Close-up view of the P1 substrate
pocket. Amino acids that line the pocket are labeled and colored
orange. InsP[6] is shown as in (B) to demonstrate the position
of the catalytic site with respect to the InsP[6]-binding site.