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. Author manuscript; available in PMC: 2019 Dec 27.
Published in final edited form as: J Am Chem Soc. 2019 Sep 13;141(38):15092–15101. doi: 10.1021/jacs.9b06064

Figure 1. Structure and major conformational states of the c-Src kinase.

Figure 1.

Cartoon representation of the chicken c-Src kinase domain structure (pdb id 5K9I). The sequences of chicken and human c-Src kinase domains differ only by two amino acids: Met354 and Asp502 in chicken correspond to Thr357 and Glu505 in human, respectively. αC-helix, A-loop, and C-loop are colored orange, red and blue, respectively. Important residues discussed in this work are shown, Asp404, Phe405 (on DFG motif); Glu310 (αC-Glu); Lys295 (catalytic Lys); Met314, Leu325, His384, and Phe405 (R-spine); Arg385 and Arg409 (able to interact with αCGlu). A diagram indicates the four types of conformational states a kinase can adopt.