Aldose Reductase NADPH Complex Crystal Structure at 2.75 Angstroms

A 2.75 Angstrom crystal structure of the recombinant human aldose reductase Cys-298 to Ser mutant complexed with NADPH. The structure was determined by David W. Borhani of BioCryst Pharmaceuticals in the United States. The description details the enzyme's beta/alpha-barrel architecture and the large conformational change upon coenzyme binding.

Use Cases

• Modeling protein-ligand interactions based on the described NADPH binding conformation.
• Analyzing enzyme conformational changes based on the described reorientation of loop 7.
• Studying inhibitor sensitivity based on the described kinetic behavior of the mutant enzyme.
• Comparing coenzyme-binding domains based on the described similarity to FAD-dependent oxidoreductases.

Strengths

• Structure resolved at a specific 2.75 Angstrom resolution.
• Describes a specific mutant (Cys-298 to Ser) with documented kinetic properties.
• Provides detailed structural observations, such as the absence of disulfide bridges and the beta/alpha-barrel fold.

Limitations

• Row count and column-level documentation are absent; field semantics must be inferred after download.
• Last update date is unknown; freshness unverified.
• Data may reflect the specific experimental bias inherent to the single structure from paperswithcode.

Provenance

Source

David W. Borhani, BioCryst Pharmaceuticals (United States)

Collection Method

X-ray crystallography, as described in the paper.