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Figure 4
Electron density for FabH ligands. OCoA is shown as black sticks and labeled FabH active-site residues as white sticks. The σA-weighted mFoDFc maps are shown at +3σ in green and −3σ in red as 5 Å bricks for (a) omitted OCoA, Cys112 Cβ and sulfur or (b) Cys112 Cβ, sulfur and acetyl group. (a) is Ac-FabH + OCoA and (b) is FabH + OCoA. Note that a water molecule takes the place of the acetyl-cysteine carbonyl.

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X
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