Crystal Structure of FimH with a Fluorinated Mannoside Ligand

N-HSQC NMR analysis provides data on the interaction between the FimH protein and a fluorinated mannoside ligand. The dataset was contributed by R.P. Jakob from the University of Basel. Fluorination of the ligand is noted to improve pharmacokinetic parameters predictive for oral availability.

Use Cases

• Analyzing protein-ligand binding interactions based on NMR spectroscopy data.
• Studying the effects of fluorination on ligand binding affinity and specificity.
• Modeling pharmacokinetic parameters for orally available drug candidates based on structural data.

Strengths

• Data originates from N-HSQC NMR analysis, a standard technique in structural biology.
• Focuses on a specific, well-defined protein-ligand complex (FimH with a tetrafluorinated biphenyl alpha D-mannoside).

Limitations

• Description metadata is limited; actual data quality requires manual inspection after download.
• Column-level documentation is absent; field semantics must be inferred after download.
• Row count is unknown, which may limit suitability assessment.

Provenance

Source

University of Basel

Collection Method

N-HSQC NMR analysis of a crystallized protein-ligand complex.