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Figure 7
Interactions at the interface of the intertwined dimer of v-Src SH3 W95R-I96T (PDB entry 7net). The residues in the different chains of the dimer are coloured grey (chain A) and green (chain B). The structure of the v-­Src SH3 Q128R mutant (yellow; PDB entry 7ner) is overlaid on one of the dimer chains. The mutated residues, Trp95 and Ile96, are shown as sticks. The Thr96(A)/Thr98(A) residues form a hydrogen bond mediated by a water molecule (W) to the symmetry-related Thr96(B)/Thr98(B) residues. For the sake of clarity, these symmetry-related residues are not represented. Asp99 show a double conformation, which facilitates intra-chain hydrogen bonds with different residues in the RT loop.

Journal logoSTRUCTURAL
BIOLOGY
ISSN: 2059-7983
Volume 77| Part 6| June 2021| Pages 854-866
https://doi.org/10.1107/S2059798321004344
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