Fig. 1
From: Structural insights into substrate recognition by the SOCS2 E3 ubiquitin ligase
Structural and interaction detail of the SBC-EpoR co-crystal. a Domain and subunit arrangement of the SBC-EpoR co-crystal. Protein chains are shown in cartoon, with EloB (cyan), EloC (magenta) and SOCS2, comprising of SOCS box (yellow) and SH2 domain (green). The EpoR_pY426 peptide is shown in orange stick. b The Fo-Fc ligand omit map of the EpoR_pY426 peptide (green mesh) contoured at 2.0 σ level to highlight densities for the EpoR_pY426 peptide (orange stick). c Hydrogen bond interactions (dash) between the pY of EpoR_pY426 peptide (orange stick) and SOCS2 residues (green stick). d Hydrogen bond interaction (dash) between the EpoR_pY426 peptide (orange stick), SOCS2 (green stick) and water (red sphere). e Hydrophobic interaction between EpoR_pY426 peptide (orange stick) and SOCS2 (surface). Hydrophobic residues on SOCS2 are colored in pink
