Supplementary Figure 2: Individual structures for all OGT–substrate complexes including electron density maps. | Nature Structural & Molecular Biology

Supplementary Figure 2: Individual structures for all OGT–substrate complexes including electron density maps.

From: The active site of O-GlcNAc transferase imposes constraints on substrate sequence

Supplementary Figure 2

Unbiased Fo-Fc difference electron density for ligands (UDP-5S-GlcNAc and peptide) contoured at 2.25 σ (a, b) or contoured at 3.5 σ after NCS averaging (c, d). E, f Previously reported OGT substrate complexes (PDB ID 4AY6, Schimpl, M. et al., Nat.Chem.Biol. 8: 969, 2012; and PDB ID 4GYY, Lazarus, M.B. et al., Nat.Chem.Biol. 8: 966-968, 2012). The entire sequence of the peptides used in the study is given; underlined residues are represented in the final model, and the amino acid in bold is the O-GlcNAc-modified serine or threonine.

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