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. 2015 Mar 30;290(20):12879–12898. doi: 10.1074/jbc.M114.634493

TABLE 1.

SOS1 residues involved in the formation of the interaction interfaces with Ras at the catalytic and allosteric sites, respectively

Residues at the SOS1 interfaces were identified by using the Sppider server with default settings. Residue numbers are based upon the SOS1 crystal structure (PDB code 1XD2), which was used for analysis.

Catalytic Ras (1XD2, chain B) interface with SOS1 (chain C); residues on Sos1 at right Glu-589, Lys-602, Trp-809, Thr-810, Lys-814, Leu-822, Ile-825, Arg-826, Thr-828, Thr-829, Thr-832, Leu-833, Glu-836, Val-875, Ser-876, Asn-879, Ser-880, Ser-881, Tyr-884, His-905, Ser-908, Asp-910, His-911, Tyr-912, Lys-913, Phe-929, Gly-931, Leu-934, Thr-935, Asn-936, Leu-938, Lys-939, Thr-940, Glu-942, Gly-943, Asn-944, Pro-945, Leu-948, Arg-950, Ser-959, Lys-963, Glu-966, Ile-967, Glu-1002, Lys-1003, Thr-1006, Asp-1007, Phe-1010, Arg-1019
Allosteric Ras (1XD2, chain A) interface with SOS1 (chain C); residues on Sos1 at right Gly-597, Ile-598, His-616, Met-617, Ala-619, Asp-620, Pro-621, Asn-622, Val-624, Lys-679, Gln-683, Pro-684, Leu-687, Arg-688, Asn-691, Arg-694, His-695, Ala-725, Lys-728, Trp-729, Ser-732, Arg-739, His-750, Asn-751, Ile-752, Thr-753, Phe-754, Gln-755, Arg-920, Ser-921, Ile-922, Asn-923, Pro-924, Gln-973, Tyr-974, Asn-976, Gln-977, Pro-978