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.

本数据集针对严重急性呼吸综合征冠状病毒2（SARS-CoV-2）的ORF10蛋白开展了全面的计算分析，重点聚焦其两个结合口袋P₀与P₁。本研究借助先进计算工具评估了该蛋白关键的理化性质与结构特征，为解析其功能角色与治疗潜力提供了见解。数据集包含结合口袋的多项详细量化指标，涵盖体积、表面积、深度、成药性评分、疏水性以及氢键结合潜力。结合口袋P₀被确定为主要结合位点，其尺寸更大（体积：164.67 埃³，表面积：463.76 埃²），疏水性更强（疏水比：0.73），且成药性评分更优（0.29）。上述特性使P₀尤为适配结合较大配体与疏水性分子，使其成为药物开发极具潜力的靶点。此外，相较于P₁，P₀的深度略深且包裹性更强，这或可增强其稳定配体结合的能力。与之相对，结合口袋P₁尺寸更小（体积：122.82 埃³，表面积：327.04 埃²），且疏水比更低（0.5）。尽管P₁的疏水相互作用能力较弱（疏水相互作用位点数量为19，而P₀为44），但它可通过更多的氢键受体位点（16个，P₀为13个）进行补偿，这表明其可能参与极性或混合型分子相互作用。尽管相较于P₀，P₁仅起到次要作用，但它仍可作为特定分子相互作用的辅助位点。序列覆盖度图、IDDT图以及接触图谱等可视化结果为ORF10内部的结构组织与残基间相互作用提供了额外的背景信息，为研究发现提供了支撑。数据集同时包含PDB格式的结构文件，可供研究者对本研究结果开展进一步探索与验证。综合来看，这些数据有助于更深入地理解ORF10在病毒-宿主相互作用中的功能，并凸显其作为治疗靶点的潜力。如需获取数据集的完整细节与访问权限，请参阅配套的Figshare知识库（https://doi.org/10.6084/m9.figshare.28738289）。本研究强调了P₀作为药物开发核心靶点的重要性，同时也认可了P₁在分子识别与功能发挥中的辅助互补作用。