Beyond the Predicted Fold: subunit-resolved binding-site fidelity of AlphaFold2-Multimer hemoglobin models

This deposit contains processed datasets from a comparative molecular docking study investigating binding-site fidelity and docking reliability in AlphaFold2-Multimer hemoglobin predictions. Human deoxyhemoglobin (PDB: 2HHB, T-state, 1.74 Å) was used as the crystal reference. Eugenol (PubChem CID 3314) and esculin (PubChem CID 5281417) were docked into the alpha and beta subunits of both the crystal and AF2-Multimer structures using AutoDock 4.2, comprising 24 docking experiments (D1–D24). Processed outputs include per-residue displacement values, binding pocket characterisation, docking results, Tanimoto similarity scores, and PCA coordinates.