Figure 2.
Fig. 2. a, simulated-annealing omitted F[o] F[c] map
of coenzyme A. The map was contoured at 3 sigma. b, the
interactions between coenzyme A and GlcB. The coenzyme A is
shown in white, and the carbons of the interacting amino acids
are in gold. The malate and magnesium ion in the active site are
also shown. c, binding of coenzyme A to the active site of GlcB.
Surfaces were made around the protein atoms and colored
according to the electrostatic potential, red for acidic, and
blue for basic residues, and were made using the program SPOCK
(66). Mg2+ in the active site is shown as a blue sphere.
F[c] map
of coenzyme A. The map was contoured at 3 sigma. b, the
interactions between coenzyme A and GlcB. The coenzyme A is
shown in white, and the carbons of the interacting amino acids
are in gold. The malate and magnesium ion in the active site are
also shown. c, binding of coenzyme A to the active site of GlcB.
Surfaces were made around the protein atoms and colored
according to the electrostatic potential, red for acidic, and
blue for basic residues, and were made using the program SPOCK
(66). Mg2+ in the active site is shown as a blue sphere.