 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
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![[Figure 2]](kw5076fig2mag.jpg)
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Figure 2
The dCK–F1–UDP complex structure reveals that two molecules of F1 bind to dCK in a parallel manner. (a) The dCK–F1–UDP complex crystallized as a dimer. Protomers A and B of dCK are represented as a cartoon diagram in light and dark green colors, respectively. F1 molecules are depicted in red. This inhibitor binds to the nucleoside-binding site of dCK in a dimeric fashion and not to the nucleotide-binding site, which is occupied by UDP (magenta). (b) Two F1 molecules (thick green sticks) bind to dCK; the molecule binding deeper into the binding cavity is referred to as F1-P1, while the second molecule is referred to as F1-P2. Residues from dCK implicated in the F1 hydrogen-bond network are represented as thin green sticks. This involves residues Glu53, Gln97 and Asp133 that contact the pyrimidine ring of F1-P1, while F1-P2 makes only one polar contact with dCK via residue Glu197. Amino acids depicted in magenta are hydrophobic residues also involved in F1 binding to dCK. Dashed lines represent hydrogen bonds and distances are in Å. Two water molecules also interact with F1 and are represented as blue spheres. |
![[Figure 2]](kw5076fig2.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
