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. 2021 Oct 28;49(20):11810–11822. doi: 10.1093/nar/gkab934

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© The Author(s) 2021. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial License (https://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com

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Figure 1. — Overall structure of human PUS7. (A) Crystal structure of PUS7(Δ1−98) is shown in cartoon representation and color-coded according to its domain architecture as labeled. The catalytic D294 residue is shown in sticks and marked with an asterisk. (B) Overlay of PUS7(Δ1−98), color-coded same as (A), and Escherichia coli TruD (gray) (PDB: 1SB7). (C) Overall best-scored predicted model of PUS7-tRNA^Gln complex. Electrostatic surface potential representation of PUS7(Δ1−98) shown in similar orientation as (A), docked with tRNA^Gln (yellow). The target U13 in tRNA^Gln is highlighted in red. PUS7 surface color indicates electrostatic potential ranging from − 10 kT/e (red) to + 10 kT/e (blue). Electrostatic surface potentials were calculated in APBS (36).