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. 2021 Jul 19;10:e66657. doi: 10.7554/eLife.66657

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© 2021, Miller et al

This article is distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use and redistribution provided that the original author and source are credited.

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Figure 4. — (A) Overall fold, a-helices colored in orange and β-strands colored in purple. (B) Comparison between SaFrmB (orange) and its closest human ortholog, ESTD (gray). Active site residues denoted in orange spheres. (C, D) Docking of substrate 1O (sticks) in the active site of FrmB. surface view, red indicates highly hydrophobic and white hydrophilic residues. Surface view (C) or stick view with catalytic triad (D).

Figure 4—source data 1. Summary of crystallographic data collection and refinement statistics.

elife-66657-fig4-data1.xlsx^{(9.8KB, xlsx)}

Figure 4—figure supplement 1. — (A) Overall fold, a-helices colored in orange and β-strands colored in purple. (B) Comparison between SaFrmB (orange) and its closest human ortholog, ESTD (gray). Active site residues denoted in orange spheres. (C, D) Docking of substrate 1O (sticks) in the active site of FrmB. surface view, red indicates highly hydrophobic and white hydrophilic residues. Surface view (C) or stick view with catalytic triad (D).

Figure 4—source data 1. Summary of crystallographic data collection and refinement statistics.

elife-66657-fig4-data1.xlsx^{(9.8KB, xlsx)}