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. 2019 Feb 13;10(12):3573–3585. doi: 10.1039/c8sc05212c

Fig. 3. Co-crystal structures of full-length Akt in complex with different covalent-allosteric inhibitors, 2Fo–Fc maps contoured at 0.8σ. (A) Co-crystal structure of Akt with 24b (PDB: ; 6HHJ) and (B) with 27 (PDB: ; 6HHG) revealed novel binding mode while labeling Cys310. (C) Co-crystal structure of Akt with 30b (PDB: ; 6HHI) and (D) with 31 (PDB: ; 6HHH) exhibited similar binding mode to borussertib while labeling Cys296.

Fig. 3