OAS1 Enzymatic Mechanism with Crystallographic Data and Metal Ion Analysis

563.6 KB of crystallographic data in PDB format, detailing the enzymatic mechanism of 2′-5′-Oligoadenylate synthetase 1 (OAS1). The dataset, authored by Pavel Kats and last updated in April 2026, integrates structural, kinetic, and quantum chemical analyses to explain antiviral immune activation.

Use Cases

• Modeling protein-ligand interactions based on crystallographic data of postreactive complexes.
• Analyzing the role of divalent metal ions (Mg2+, Mn2+) in catalysis based on kinetic data.
• Investigating quantum mechanical effects in enzyme function based on quantum chemical analyses.
• Comparing substrate binding kinetics based on the described 9-fold rate increase with Mn2+ substitution.

Strengths

• Includes crystallographic data (PDB format) revealing postreactive complex geometry.
• Integrates structural, kinetic, and quantum chemical analyses for a multi-faceted mechanism.
• Highlights a specific 9-fold increase in substrate binding rate with Mn2+ ions.

Limitations

• Row count is unknown, which may limit suitability assessment.
• Column-level documentation is absent; field semantics must be inferred after download.
• Data may reflect methodological bias inherent to the specific experimental and computational techniques used.

Provenance

Source

figshare

Collection Method

Generated from crystallographic, kinetic, and quantum chemical analyses as part of a research study.

Time Range

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Freshness

Last updated 2026-04-13 10:04:01; freshness should be verified.

Geography

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