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. Author manuscript; available in PMC: 2020 Jul 18.
Published in final edited form as: ACS Chem Biol. 2019 Oct 7;14(10):2264–2275. doi: 10.1021/acschembio.9b00610

Figure 4.

Figure 4.

Structural rationale for negatively charged residues in the seventh CTD position directing ABL1 phosphorylation of Tyr1. (A) Structure of ABL1 (light blue) bound to an ATP-peptide bisubstrate analog (dark green) based on the SRC sequence (PDB: 2G1T). The ABL1 surface is represented as a gray transparent layer around the protein. (B) Electrostatic region of ABL1 preceding the nitrophenylalanine binding pocket (blue−positive, red−negative). (C,D) Modeling of a phosphoserine mimic or phosphoserine (Glu or pSer, respectively; white) into the Ile106 position of the ATP-peptide bisubstrate analog. The most likely rotamer for Glu and pSer was selected for modeling. Predicted salt bridges between the modeled Glu/pSer and Arg367 of ABL1 are shown in yellow.