Figure 2.
Figure 2. The 20 lowest-energy solution structure of the human
ACC2 biotinoyl domain (residues 891-964). A: Twenty structures
of hACC2 biotinoyl domain are superimposed (residue range for
r.m.s.d. calculation and matching is 895-960). The backbone
region was well converged, and the r.m.s.d. was 0.23 Å. B:
Ribbon representation of the hACC2 biotinoyl domain. The two
-sheets
are orange and green, respectively. C: Side chains of
hydrophobic residues involved in forming the hydrophobic core.
D: Five bifurcated hydrogen bonds (dotted lines) stabilize the
-sandwich
structure.
The above figure is reprinted
by permission from John Wiley & Sons, Inc.:
Proteins
(2008,
72,
613-624)
copyright 2008.
-sheets
are orange and green, respectively. C: Side chains of
hydrophobic residues involved in forming the hydrophobic core.
D: Five bifurcated hydrogen bonds (dotted lines) stabilize the