OAS1 Enzymatic Mechanism with Crystallographic and Kinetic Data

A figshare dataset by Pavel Kats, last updated in April 2026, provides structural and kinetic data on 2′-5′-Oligoadenylate synthetase 1 (OAS1). The 541.7 KB dataset includes crystallographic data of postreactive complexes and kinetic analyses revealing a 9-fold increase in substrate binding rate with Mn2+ ions. This study integrates quantum chemical analyses to elucidate the role of metal ions in the catalytic cycle.

Use Cases

• Modeling protein-ligand interactions based on crystallographic data of OAS1 postreactive complexes.
• Analyzing the kinetic impact of metal ion substitution (Mg2+ to Mn2+) on substrate binding rates.
• Studying the proposed role of a third transient metal ion in the catalytic mechanism.
• Investigating quantum mechanical effects in enzymatic function for the OAS/cGAS family.

Strengths

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

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 (541.7 KB), indicating limited scope.

Provenance

Source

figshare

Collection Method

Data generated from structural, kinetic, and quantum chemical analyses as described in the study.

Time Range

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Freshness

Last updated 2026-04-13 10:03:57; freshness should be verified.

Geography

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