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Figure 1.
Fig. 1. Structure and electron density for the
acyl-intermediate near the substrate binding cleft at 0.
95-Å resolution. A, 2F[obs]  F[calc]
electron density map contoured to 1.7  (blue) and
4.0 (gold).
The blue contour level was chosen such that atoms with 60%
occupancy become visible in the active site. The structural
model for the enzyme moiety is green, with the exception of the
oxygen and nitrogen atoms of the catalytic histidine and serine,
which are colored red and blue, respectively. The acyl-peptide
moiety is colored orange. B, least square superposition of the
0.95-Å acyl-intermediate structure (cyan) and the
1.1-Å native elastase structure (green).
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