Top-Scoring Protein-Ligand Complex Interaction Summary

A summary of molecular interactions for top-scoring docked protein-ligand complexes. The data includes hydrogen-bonding residues, hydrophobic and hydrophilic contacts, salt bridges, water-mediated hydrogen bonds, and π–π stacking interactions. It was created by Kamal A. Qureshi and published on the figshare platform in April 2026.

Use Cases

• Validate docking poses by analyzing reported hydrogen-bonding residues and salt bridges against known binding site data.
• Benchmark interaction analysis pipelines using the detailed contact types like hydrophobic (C···C/S) and hydrophilic interactions.
• Study the prevalence of water-mediated hydrogen bonds and π–π stacking interactions in high-scoring complexes.
• Analyze interaction distances (reported in Å) and residue contact ranges to understand binding geometry.

Strengths

• Includes multiple specific interaction types: hydrogen bonds, hydrophobic contacts, salt bridges, and π–π stacking.
• Interaction distances are quantified in Ångströms, and ranges are provided for multiple contacts.

Limitations

• The dataset is very small at 9.5 KB, indicating a limited number of complexes or interactions.
• Rows and total complex count are unknown, limiting assessment of statistical power.
• π–π stacking interactions were identified via visual inspection, which may introduce subjectivity.

Provenance

Source

figshare, author Kamal A. Qureshi.

Collection Method

Generated using a Python-based interaction analysis pipeline inspired by PLIP, applied to top-scoring docked complexes.

Freshness

Last updated in April 2026.