OAS1 Crystallographic Data for Enzymatic Mechanism Analysis

Pavel Kats provides crystallographic data of OAS1 postreactive complexes, published on figshare in April 2026. The 550.2 KB dataset in PDB format details the enzymatic mechanism of 2′-5′-Oligoadenylate synthetases (OAS), integrating structural, kinetic, and quantum chemical analyses. It reveals the role of divalent metal ions and quantum effects in activating antiviral innate immune responses.

Use Cases

• Analyzing the geometry of OAS1 following product formation and dissociation based on crystallographic data.
• Studying the role of divalent metal ions in catalysis based on structural and kinetic analyses.
• Investigating quantum mechanisms in enzyme function based on integrated quantum chemical analyses.
• Comparing catalytic efficiency with different metal ions based on the described 9-fold increase in substrate binding rate with Mn2+ substitution.

Strengths

• Data integrates structural, kinetic, and quantum chemical analyses for a detailed mechanism.
• Reveals a specific 9-fold increase in substrate binding rate when catalytic Mg2+ is substituted with Mn2+.
• Provides crystallographic data of OAS1 postreactive complexes.

Limitations

• Row count is unknown, which may limit suitability assessment.
• Column-level documentation is absent; field semantics must be inferred after download.
• The dataset is small (550.2 KB), indicating limited scope.

Provenance

Source

figshare

Collection Method

Likely contains data from crystallographic, kinetic, and quantum chemical analyses.

Time Range

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Freshness

Last updated 2026-04-13 10:03:58; freshness should be verified.

Geography

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