OAS1 Crystallographic Data on Metal Ion and Quantum Effects in Antiviral Response

Crystallographic data of OAS1 postreactive complexes reveal the geometry following product formation and a 9-fold increase in substrate binding rate when catalytic Mg2+ is substituted with Mn2+ ions. The dataset, published by Pavel Kats in 2026, provides structural, kinetic, and quantum chemical analyses of the 2′-5′-Oligoadenylate synthetase enzymatic mechanism. It is a 550.0 KB dataset containing PDB files, highlighting the role of a third metal ion and quantum mechanisms in catalysis.

Use Cases

• Modeling the catalytic cycle of OAS1 based on crystallographic data of postreactive complexes.
• Investigating the role of divalent metal ions (Mg2+, Mn2+) in enzyme activation based on kinetic analyses.
• Studying quantum mechanical effects in enzymatic function based on the integrated quantum chemical analyses.
• Analyzing product release sequences in nucleotidyltransferases based on the structural data.

Strengths

• Includes crystallographic data revealing OAS1 geometry post-catalysis.
• Kinetic analyses show a specific 9-fold increase in substrate binding rate with Mn2+ substitution.
• Integrates structural, kinetic, and quantum chemical analyses for a multi-faceted mechanism.

Limitations

• Dataset size is 550.0 KB, indicating a limited scope focused on specific structural data.
• Column-level documentation is absent; field semantics must be inferred after download.
• Row count is unknown, which may limit suitability assessment.

Provenance

Source

figshare

Collection Method

Likely contains data from crystallographic, kinetic, and quantum chemical analyses conducted for the study.

Time Range

null

Freshness

Last updated 2026-04-13 10:03:55; freshness should be verified.

Geography

null