Human Muscle Fatty Acid-Binding Protein Structure at 2.1 Å Resolution

7243 unique reflections were used to refine the three-dimensional structure of recombinant human muscle fatty acid-binding protein to 2.1 Å resolution. The refined model has a crystallographic R factor of 19.5% and reveals a single bound fatty acid molecule within the protein's interior core. The structure was determined by Giuseppe Zanotti of the University of Padua using x-ray diffraction data.

Use Cases

• Modeling protein-ligand interactions based on the described van der Waals contacts and hydrogen bonds with the bound fatty acid.
• Comparative structural analysis based on the described similarity to rat intestinal fatty acid-binding protein.
• Studying binding site evolution based on the finding that muscle and intestinal proteins have distinct binding sites.
• Analyzing protein hydration based on the seven ordered water molecules identified within the protein interior.

Strengths

• High-resolution structural data refined to 2.1 Å resolution.
• Detailed atomic-level description of protein-ligand interactions involving 13 residues and ordered water molecules.
• Direct comparison provided to a related protein structure (rat intestinal fatty acid-binding protein).

Limitations

• Row count and dataset size are 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 Padua

Collection Method

X-ray diffraction data collection and structural refinement.