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. Author manuscript; available in PMC: 2011 Mar 29.
Published in final edited form as: Drug Metab Dispos. 2008 Jun 12;36(9):1951–1959. doi: 10.1124/dmd.108.020925

Figure 4. Human DCK and CMPK structural models.

Figure 4

(A) The two monomers in the DCK dimeric crystal structure are shown as ribbon structures in two shades of blue. Bound in the active site of each monomer are ADP (orange) and deoxycytidine (dC, blue), shown as space-filling structures. The Cα atoms of the three residues altered by SNPs (Ile24, Ala119, Pro122) are drawn as purple spheres. The N- and C- termini, active site ligands, and positions of the altered residues are labeled for the right monomer. (B) The human CMPK monomer is shown as a blue ribbon structure. Bound in the active site is a sulfate ion shown as space-filling spheres. The Cα atoms of the three residues altered by SNPs (Gln48, Glu75, and Asn83) are drawn as purple spheres.