Table 1.

The position of SDP residues in the structures of the five Ras superfamily members, and their possible biological and functional implications

Family PDB chain Arf 1hurA,B Ras (Fig. 5) 121pA Rho 1a2bA Rab 2folA Ran 1l2MA 
Residues in the proximity of the GTP/GDP binding pocket Ala28, Pro47, Gly69 Ala11, Val14, Pro34, Thr58, Ala59 Asp13, Cys16, Pro36 Asp16, Val19, Leu25, Ser39 Thr21, Asp18, Ala41, Ala67 
Residues involved in protein–protein interactions Pro47, Phe51, Trp66, Val68, Gly69 Pro34, Glu37, Leu56, Ala59, Arg68 Asp13, Cys16, Leu22, Pro36, Phe39, Thr58, Thr60, Ala61, Asp67, Arg70, Arg122 Val43, Trp62, Ala65, Arg71 Asp18, Val45, Trp64, Ala67, Gly73, Arg76, Asp91 Lys127 
Residues coordinating communication between different lobes Arg75, Val91, Asp93, Pro131 Ala65, Val81, Ala83, Ala121 Asp67, Cys83, Ser85, Arg122 Arg71, Ala81, Val87, Leu89, Ala126 Gly73, Met89, Asp91, Lys127 
Conserved SDP residues with unknown function Leu25, Leu34, Trp78, Thr85 Gly75, Thr20 Thr77 Thr64, Thr74 Val27, Thr66, Ala83 
Family PDB chain Arf 1hurA,B Ras (Fig. 5) 121pA Rho 1a2bA Rab 2folA Ran 1l2MA 
Residues in the proximity of the GTP/GDP binding pocket Ala28, Pro47, Gly69 Ala11, Val14, Pro34, Thr58, Ala59 Asp13, Cys16, Pro36 Asp16, Val19, Leu25, Ser39 Thr21, Asp18, Ala41, Ala67 
Residues involved in protein–protein interactions Pro47, Phe51, Trp66, Val68, Gly69 Pro34, Glu37, Leu56, Ala59, Arg68 Asp13, Cys16, Leu22, Pro36, Phe39, Thr58, Thr60, Ala61, Asp67, Arg70, Arg122 Val43, Trp62, Ala65, Arg71 Asp18, Val45, Trp64, Ala67, Gly73, Arg76, Asp91 Lys127 
Residues coordinating communication between different lobes Arg75, Val91, Asp93, Pro131 Ala65, Val81, Ala83, Ala121 Asp67, Cys83, Ser85, Arg122 Arg71, Ala81, Val87, Leu89, Ala126 Gly73, Met89, Asp91, Lys127 
Conserved SDP residues with unknown function Leu25, Leu34, Trp78, Thr85 Gly75, Thr20 Thr77 Thr64, Thr74 Val27, Thr66, Ala83 

Numbers correspond to positions in the PDB structures (see Table S5).

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