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Figure 2.
Fig. 2. Schematic diagram of the active site of VanA from
the structure showing the interaction of various water molecules
in addition to amino acid side chains. The protein backbone of
the residues in the region of His-244 and Tyr-315 is shown as a
solid black line. Hydrogen bond distances between Tyr-315,
His-244, and the second subsite carboxyl oxygen of the
transition state inhibitor are 2.77 Å and 2.74 Å,
respectively. Two phenylalanine residues (F169 and F294) form
stacking interactions with the adenine nucleotide rings. Several
water molecules in the active site form interactions with the
phosphosphate and magnesium atoms as well as amino acid side
chains. There is an additional hydrogen bond between water 475
and water 371, which is not shown for clarity.
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