Residues are numbered sequentially and for fXa also according to chymotrypsin by parentheses.

Residues of fVa not previously listed as potential epitopes of recognition of prothrombin or fXa by a recent review of biochemical data and computational models.⁶⁶ The review lists a total of 56 residues of the A2 domain and 35 residues of the A3 domain of fVa involved in the interaction with fXa. The cryo-EM structure documents only 11 residues in the A2 domain (A511, F576, D577, T579, T626, D628, E662, E669, E672, V675, E686), 3 of which not reported previously (E662, E672, V675), 3 in the A3 domain (S1598, T1679, H1683) and 1 in the C1 domain (Y2021) also not reported previously. The main interactions are shown in Figure 4B-C. The review also lists 23 residues in the A2 domain, 18 in the A3 domain and 10 in the C1 domain as interacting with prothrombin.⁶⁶ The cryo-EM structure documents 2 residues in the A1 domain (T305, K309) not reported previously, 6 residues in the A2 domain (R505, A694, Y696, D697, Y698, L702), 4 of which (A694, Y696, D697, L702) not reported previously, and no contacts involving the A3 and C1 domains.