WhatRes scores predicted protein structures on realism, exposing over-idealised geometry
- WhatRes is a coordinate-only assessment tool that places a structure on two axes: the experimental resolution its local geometry resembles, and how realistic that geometry is compared with experimental structures of similar resolution.
- It is applied to AI-predicted models and benchmarked against experimental structures, rather than tested prospectively on a design project.
- Even confidently predicted models can look high-resolution yet show noticeably narrower spread in bond lengths and angles than real high-resolution crystal structures, so they are over-idealised.
- This is a bioRxiv preprint and has not been peer reviewed.
💡 Points Based on the abstract
Flagging a narrow bond-length spread is easy; whether it matters for us is the open question. Deposited crystal geometry is itself shaped by refinement restraints, so the "realistic" reference is partly a refinement convention. Before trusting the score, check whether it tracks docking pose recovery or pocket accuracy on models of your own targets.
Realism and resolution: How AI-predicted protein structures differ from experimental structures ↗