Pea Lectin-Trimannoside Complex X-Ray Crystal Structure at 2.6 Angstroms Resolution

A 2.6-A resolution x-ray crystal structure of pea lectin in complex with a trimannosyl core oligosaccharide, solved by molecular replacement. The structure was refined with an R factor of 0.183 for data between 8.0 and 2.6 A resolution and an average atomic temperature factor of 26.1 A2. The dataset was produced by James M. Rini from the University of Toronto.

Use Cases

• Analyzing hydrogen bonding networks based on interactions with protein residues Asp-81, Gly-99, Asn-125, Ala-217, and Glu-218.
• Studying van der Waals contact patterns based on the involvement of Phe-123 with the carbohydrate.
• Comparing binding site conformations based on the described differences between the complex and unliganded pea lectin and concanavalin A structures.
• Investigating water structure correlations based on the relationship between carbohydrate oxygen atom positions and bound water molecules.

Strengths

• High-resolution structural data at 2.6 Angstroms, providing atomic-level detail.
• Specific refinement metrics are provided, including an R factor of 0.183 and an average atomic temperature factor of 26.1 A2.
• Detailed description of molecular interactions, including specific hydrogen bonds and van der Waals contacts.

Limitations

• Row count is unknown, which may limit suitability assessment.
• Column-level documentation is absent; field semantics must be inferred after download.
• Last update date is unknown; freshness unverified.

Provenance

Source

University of Toronto

Collection Method

X-ray crystallography solved by molecular replacement.