Fig. 2: GAP domains and Ral binding of RalGAP.
From: Structure and mechanism of the RalGAP tumor suppressor complex

a Experimental structures of the Asn-Thumb GAP domain of RGα2 and b the pseudo-GAP domain of RGβ in the same orientation. c Model of GTP-bound RalA associated with RGα2 based on an AlphaFold 3 prediction. d Close-up of the active site. The catalytically relevant amino acids RGα2N1742 and RalY43 are positioned like the equivalent residues in the structure of the Rap-RapGAP complex.