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. 2023 Feb 11;4(4):100559. doi: 10.1016/j.xplc.2023.100559

Figure 2.

Figure 2

Structural and biochemical characteristics of FER-KD and its mutants.

(A) Western blotting analysis of the phosphorylation state of FER-KD, FER-KDS525A, and FER-KDK565R. CK represents 1 mM FER-KD samples incubated with 1 mM ATP and 10 mM Mg2+ at 25°C for 30 min.

(B) ATPase activity of FER-KD, FER-KDS525A, and FER-KDK565R.

(C) Ribbon structural comparison of the FER-KD–ADP (green), FER-KDS525A–ADP (cyan), FER-KDK565R–ADP (orange), and FER-KDK565R–ATP (pink) complexes, which gives Cα RMSDs of 0.230, 0.280, and 0.187 Å, respectively.