Fig. 6: Effects of the second-sphere residues on the binding modes of nucleotide halogenases.
From: Discovery and substrate specificity engineering of nucleotide halogenases
a Percentage of binding modes for CtNTHWT and CtNTHH274Y. b Percentage of binding modes for AdaVWT and AdaVF303V. c Representative structure of binding mode 2 for CtNTHH274Y/dAMP; Tyr274 form a stable water-bridged hydrogen bonding interaction with 3′-OH group of dAMP (highlighted in the dotted cycle). d Representative structure of binding mode 1 for CtNTHH274Y/dGMP; Tyr274 positions Phe272 to be closer to the sugar-binding site, making the deoxyribose ring of dGMP to get farther away from the catalytic iron center.
