SIMORGH: Ensemble-Aware Geometric Deep Learning for Apo-State and Cryptic Ligand Binding Site Prediction
Mokhtari, O.; Naghsh Nilchi, A.; Grüning, B.; Karami, Y.; Khakzad, H.
Show abstract
Most computational methods identify protein-ligand binding sites from ligand-bound (holo) protein structures, where the binding pocket is already preorganized. Although convenient for benchmarking, this setting differs from the practical drug discovery scenario, in which binding sites must be inferred from ligand-free (apo) proteins. In fact, binding-competent conformations may represent only a subset of the accessible structural ensemble, while transient and cryptic pockets can emerge through conformational fluctuations. Consequently, prediction from a single static structure is often insufficient. Here we present SIMORGH, an ensemble-aware SE(3)-equivariant geometric learning framework that predicts ligand binding sites by integrating information across protein conformational ensembles. SIMORGH employs a two-stage architecture consisting of a structure-level equivariant encoder that learns geometric representations from individual conformations and a lightweight ensemble-level aggregation module that combines them into residue-level binding predictions while scaling near-linearly with both protein and ensemble size. We evaluate SIMORGH across multiple complementary settings, including the PLINDER apo benchmark, molecular dynamics trajectories spanning more than 200 cryptic-pocket proteins, and established community benchmarks. SIMORGH consistently outperforms existing static and dynamics-aware methods under the challenging ligand-free setting, while identifying cryptic binding pockets, maintaining strong prediction consistency between paired apo and holo structures, and scaling efficiently to large multi-chain complexes. To facilitate reproducible, transparent, and accessible use, Simorgh is available through the Galaxy Europe server (https://usegalaxy.eu).
Matching journals
The top 5 journals account for 50% of the predicted probability mass.
Similar papers in this journal
- AlphaFold as a Prior: Experimental StructureDetermination Conditioned on a Pretrained Neural Network 95%
- OpenFold: Retraining AlphaFold2 yields new insights into its learning mechanisms and capacity for generalization 94%
- SurfDock is a Surface-Informed Diffusion Generative Model for Reliable and Accurate Protein-ligand Complex Prediction 94%
Similar papers in this journal
- Hybrid Deep Learning with Protein Language Models and Dual-Path Architecture for Predicting IDP Functions 95%
- InversePep: Diffusion-Driven Structure-Based Inverse Folding for Functional Peptides 94%
- ProDualNet: Dual-Target Protein Sequence Design Method Based on Protein Language Model and Structure Model 93%
"Similar papers" are the closest papers from that journal in the model's embedding space. They show what the match is built on, but the ranking comes mostly from a classifier over the whole training set, not from these examples alone.