Skip to main content
. Author manuscript; available in PMC: 2011 Mar 11.
Published in final edited form as: Nat Struct Mol Biol. 2009 Aug 30;16(9):979–986. doi: 10.1038/nsmb.1663

Figure 3. Close-up view of the polymerase active site region.

Figure 3

The fingers, palm, exonuclease, and the N-terminal domains are colored in faded yellow, cyan, magenta, and blue. The DNA is colored gray, templating G and incoming dCTP are in red, and the Ca2+ ions (A, B and C) are in green. Highlighted and labeled are the acidic residues (Asp608, Asp764 and Glu802); residues that interact with the triphosphate moiety of incoming dCTP via side chain (Arg674 and Lys701), main chain (Ser611 and Leu612), and a water molecule (Lys678); residues that impinge on the dG-dCTP bases (Asn705, Ser706, Tyr708, and Glu709); and Tyr613 that stacks against the dCTP sugar. The residues are colored to match the domain they belong to.