Skip to main content
. Author manuscript; available in PMC: 2009 Oct 13.
Published in final edited form as: Virology. 2007 May 9;366(1):126–136. doi: 10.1016/j.virol.2007.03.059

Fig. 5. Active site similarity between Pnkp phosphatase and CTD serine phosphatase.

Fig. 5

Stereo view of the phosphatase active site from Pnkp protomer D (green) superimposed on the BeF3-modified active site of CTD phosphatase Scp1 (beige). The aspartyl-BeF3 adduct is depicted with the beryllium in yellow and the fluorines colored red (reflecting their mimicry of the phosphate of the aspartyl-phosphate intermediate). The Mg2+ of Scp1 is depicted as a cyan sphere and the associated waters as red spheres. Atomic interactions in the Scp1 active site are indicated by dashed lines. Pnkp side chains are labeled.