Extended Data Fig. 4: Modeling of potential HSV-1 UL5 K342 and H342 rotamers.
From: Structural and mechanistic insights into herpesvirus helicase–primase and its therapeutic inhibitors
a, Cryo-EM structure of the HSV-1 HP complex with PTV at the binding site, showing PTV and UL5 residues N342, N343, and Y882 as stick representations. b, Same structure as in (a), showing two representative modeled conformations of K342: an energetically favorable conformation in cyan, and a less favorable conformation in orange. c, Same structure as in (a), showing the modeled conformation of H342 as sticks in cyan. Key distances between closely contacting atoms are represented as dashed lines, with measurements provided in Å.
