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. 2024 Apr 10;10(15):eadk8157. doi: 10.1126/sciadv.adk8157

Fig. 4. Structure of combYSelect1 and combYSelect2.

Fig. 4.

(A) X-ray crystal structure (2.5 Å) highlighting the T411Y/K409S and L368S/D399Y mutations. The tyrosines are dynamic with two conformations modeled for T411Y at 67% (T411YA) and 33% (T411YB) occupancy and for D399Y at 42% (D399YA) and 58% (D399YB) occupancy. (B) X-ray crystal structure (3 Å) highlighting the T411Y/K409S and D399Y/K447S mutations. The tyrosines are dynamic with two conformations modeled for D399Y at 38% (D399YA) and 62% (D399YB) occupancy. N390 and Y407 are nearby residues involved in the interactions.