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. 2008 Aug 4;105(32):11116–11121. doi: 10.1073/pnas.0804754105

Fig. 3.

Fig. 3.

Structure of a small-molecule inhibitor bound to the β-clamp. (A) The RU7 compound. (B) Distances between RU7 and the β-clamp. Side-chain movements upon binding RU7 are indicated. Yellow and white are residues of β in the absence or presence of RU7, respectively. Distances between RU7 and protein residues are marked in black; the distances 3.73, 3.41, and 3.03 Å are marked a, b, and c, respectively.