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Figure 2
Electron density for CATIII ligands in the active sites in molecules A (a), B (b) and C (c) in the trimer. AcOCoA or OCoA is shown as black sticks, chloramphenicol is shown as white sticks and CATIII active-site residues are labeled and shown as gray sticks. The water participating in the oxyanion hole and hydrogen-bonded to chloramphenicol is circled in red. The σA-weighted mFoDFc maps for omitted ligands are shown at +3σ in green and −3σ in red as 5 Å bricks. The Ser142 side-chain hydroxyl was also omitted in order to judge occupancy. Note that a water molecule close to the ester O atom in (a) lies in a similar position as a partially occupied water in (c), revealing some presence of OCoA in (a).

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X
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