REFINEMENT OF THE STRUCTURE OF RECOMBINANT RAT INTESTINAL FATTY ACID-BINDING APOPROTEIN AT

A 1.19-angstrom resolution X-ray crystallography model of the 131-residue rat intestinal fatty acid-binding protein without bound ligand. The refined model includes 237 solvent molecules, alternate conformers for 228 protein atoms, and details on 10 beta-strands and 2 alpha-helices. Giovanna Scapin from the Albert Einstein College of Medicine authored the associated research paper.

Use Cases

• Analyzing protein-ligand binding site dynamics based on the described multiple conformations of aromatic side-chains.
• Studying solvent structure and hydrogen bonding networks based on the 237 identified solvent molecules.
• Refining protein structure prediction models based on high-resolution atomic coordinates and bond angle deviations.
• Investigating the structural basis of ligand binding in proteins lacking a true hydrophobic core.

Strengths

• High-resolution structural data refined to 1.19 angstroms.
• Detailed model includes 237 solvent molecules and alternate conformers for 228 protein atoms.
• Specific structural metrics are provided, including an R-factor of 16.9% and RMS deviations for bond lengths and angles.

Limitations

• Row count and column-level documentation are unknown, which may limit suitability assessment.
• Last update date is unknown; freshness unverified.
• The dataset license is closed, restricting reuse.

Provenance

Source

Albert Einstein College of Medicine (author: Giovanna Scapin)

Collection Method

X-ray crystallography refinement of recombinant protein structure.