Structural and Functional Analysis of SARS-CoV-2 ORF10 Protein Binding Pockets

This dataset provides a comprehensive computational analysis of the SARS-CoV-2 ORF10 protein, focusing on its two binding pockets, P_0 and P_1. The study leverages advanced computational tools to evaluate key physicochemical properties and structural characteristics, offering insights into their functional roles and therapeutic potential.

The dataset includes detailed metrics on the binding pockets, such as volume, surface area, depth, druggability scores, hydrophobicity, and hydrogen bonding potential. Pocket P_0 is identified as the primary binding site, characterized by its larger size (volume: 164.67 ų, surface area: 463.76 Ų), higher hydrophobicity (hydrophobicity ratio: 0.73), and superior druggability score (0.29). These attributes make P_0 particularly suitable for accommodating larger ligands and binding hydrophobic molecules, positioning it as a promising target for drug discovery. Additionally, P_0 is slightly deeper and more enclosed than P_1, which may enhance its ability to stabilize ligand binding.

In contrast, pocket P_1 is smaller (volume: 122.82 ų, surface area: 327.04 Ų) and exhibits a lower hydrophobicity ratio (0.5). While P_1 has a reduced capacity for hydrophobic interactions (19 vs. 44 in P_0), it compensates with a higher number of hydrogen bond acceptors (16 vs. 13 in P_0), suggesting its potential involvement in polar or mixed-type interactions. Although P_1 plays a secondary role compared to P_0, it may still serve as an auxiliary site for specific molecular interactions.

The findings are supported by visualizations such as sequence coverage plots, IDDT plots, and contact maps, which provide additional context on the structural organization and residue-residue interactions within ORF10. Structural files in PDB format are also included, enabling further exploration and validation of the results. Together, these data contribute to a deeper understanding of ORF10's role in viral-host interactions and highlight its potential as a therapeutic target.

For full details and access to the dataset, refer to the accompanying Figshare repository (https://doi.org/10.6084/m9.figshare.28738289 ). This work underscores the importance of P_0 as the dominant site for drug discovery efforts while acknowledging the complementary role of P_1 in molecular recognition and function.