Extended Data Fig. 7 | Accuracy of predictions for interfaces. Protein–
protein interaction is an important domain for understanding protein function
that has hitherto largely been limited to template-based models because of the
need for high-accuracy predictions, although there has been moderate
success^54 in docking with predicted structures up to 6 Å r.m.s.d. This figure
shows that the predictions by AlphaFold improve accuracy in the interface
regions of chains in hetero-dimer structures and are probably better
candidates for docking, although docking did not form part of the AlphaFold
system and all submissions were for isolated chains rather than complexes. For
the five all-groups heterodimer CASP13 targets, the full-atom r.m.s.d. values of
the interface residues (residues with a ground-truth inter-chain heavy-atom
distance <10 Å) are computed for the chain submissions of all groups (green),
relative to the target complex. Results >8 Å are not shown. AlphaFold (blue)
achieves consistently high accuracy interface regions and, for 4 out of 5
targets, predicts interfaces below <5 Å for both chains.