What researchers are trying
IsoDDE jointly predicts biomolecular structure and ligand-induced conformational change, including blind pocket identification from sequence and ligand-conditioned opening of hidden sites.
Finding cryptic pockets from sequence
Can a model reveal ligandable pockets that are hidden in the unbound protein and only open after a ligand or allosteric change?
Why it matters
Cryptic pockets could make previously undruggable interfaces and allosteric sites experimentally actionable without starting from a known bound structure.
Evidence boundary
The public evidence is currently a company technical report and benchmark narrative. Prospective medicinal-chemistry validation and independent replication remain essential.
Organizations represented
Isomorphic Labs
Demonstrated evidence
What has actually been shown.
- Developer-reported opening of a cryptic pocket at the NKG2D interface.
- Developer-reported identification of known and proposed allosteric pockets in cereblon from sequence before ligand co-folding.
Unresolved questions
- How often are predicted pockets experimentally ligandable rather than geometrically plausible?
- How robust is pocket discovery across membrane proteins, intrinsically disordered regions and low-data target families?
- Can calibrated confidence distinguish genuine induced pockets from model hallucinations?
Signals to watch next
- Technical-report updates
- Prospective hit discovery
- Independent cryptic-pocket benchmarks
- Public structures and affinity data
Connected evidence graph
Related BioAtlas model passports.
AlphaFold 2 / 3
The model that solved the 50-year protein-folding problem.
4/7 evidence fields documentedBoltz-1 / Boltz-2
Open-source AF3-quality structure — plus binding affinity.
4/7 evidence fields documentedDiffDock
Reframing molecular docking as a diffusion generative problem.
4/7 evidence fields documentedNeuralPLexer / Enchant
Physics-aware structure + multi-task ADMET foundation models.
2/7 evidence fields documentedPrimary and evaluation sources