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. 2021 Jun 18;12:3788. doi: 10.1038/s41467-021-24083-y

Fig. 4. Structure of RON13.

Fig. 4

a Cryo-EM density map determined by single-particle analysis at a resolution of 3.1 Å (top), and the corresponding views of the atomic model of rRON13dk. The kinase domain and the C-terminal extension (CTE) are colored in orange and gray tones. b Domain organization of RON13. The position of the ATP-binding site is indicated by the ATP ligand modeled into the active site (absent in the experimentally determined density map). The N-lobe insertion (NLI, red) and the C-terminal extension (CTE, gray) are color-coded. c Surface representation of RON13 kinase domain at 3.1 Å resolution. d Comparison of RON13 kinase domain structure with other kinases. PKA from Mus musculus (PDB ID: 1atp) is complexed with MnATP and an inhibitory peptide (violet). ROP5B from T. gondii bound to ATP (PDB ID: 3q60) contains a ROP-specific N-terminal extension (blue).