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Figure 2.
Figure 2. A: Ribbon diagram of a superposition of YDR428C
(blue) and P. fluorescens carboxylesterase (grey). Residues of
the catalytic triad, shown in ball and stick, indicate the
active site location. B: Same as A, but a close up view of the
catalytic triad. Active site residues as observed in P.
fluorescens carboxylesterase (PDB 1auo; grey; P. fluorescens
residues shown in parenthesis) and their counterparts in YDR428C
(blue) are shown in ball and stick. Hydrogen bond interactions
and distances are indicated. C: Ribbon diagram of the YDR428C
dimer.  7
strands and helices H10 and H12 forming part of the dimer
interface and locations of active sites (arrow) are indicated.
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