OAS1 Enzymatic Mechanism with Crystallographic Data and Metal Ion Analysis

Crystallographic data of OAS1 postreactive complexes provides structural, kinetic, and quantum chemical analyses of this innate immune sensor. The dataset, authored by Pavel Kats and last updated in April 2026, reveals the role of three metal ions and a 9-fold increase in substrate binding rate when Mg2+ is substituted with Mn2+. The findings are pertinent to the OAS/cGAS family of sensors and a broader class of nucleotidyltransferases.

Use Cases

• Modeling the catalytic mechanism of OAS1 based on crystallographic geometry and product release order.
• Analyzing the role of divalent metal ions in enzyme catalysis based on structural and kinetic data.
• Investigating quantum effects in enzyme function based on the integrated quantum chemical analyses.
• Comparing enzymatic activity across metal ion substitutions based on the reported 9-fold binding rate increase.

Strengths

• Includes crystallographic data (PDB format) providing structural insights.
• Integrates structural, kinetic, and quantum chemical analyses for a multi-faceted view.
• Reveals a specific, quantifiable 9-fold increase in substrate binding rate with Mn2+ substitution.

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 (548.9 KB), indicating limited scope.

Provenance

Source

figshare

Collection Method

Likely contains data from crystallographic experiments and computational analyses as described in the associated study.

Time Range

The study and data were made available in April 2026.

Freshness

Last updated 2026-04-13 10:03:59; freshness should be verified.

Geography

Spatial coverage is not specified.