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Figure 1.
Fig. 1. Overall fold of FtHAP. (a) Ribbon drawing of the
FtHAP protomer. Residues are colored according to a rainbow
scheme, with blue at the N-terminus and red at the C-terminus.
The P[i] ligand is shown in spheres. The side chains of His17,
Phe23, and Tyr135 are drawn as sticks in white. Strands of the
β-sheet are numbered. The first three helices of the
polypeptide chain are labeled α1, α2, and α3. The conserved
portion of the dimerization loop (residues 116–121) is colored
magenta. (b) Ribbon and surface representations of the protomer,
highlighting domain structure. The orientation is the same as in
(a). The core domain is colored blue, and the cap domain is
colored pink. The P[i] ligand is shown in spheres, and the side
chains of His17, Phe23, and Tyr135 are drawn as sticks.
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