Oligomeric State and Activity of Truncated Bacteriophage Proteins

AlphaFold 3 predicted the 3D structures for selected truncated variants of the bacteriophage protein KP32gp38. This 5.5 KB Excel file summarizes the experimental oligomeric state and enzymatic activity results for these variants. The dataset was created by Agnieszka Latka and last updated in April 2026.

Use Cases

• Correlate specific protein variant truncations with their measured oligomeric state (e.g., dimer, trimer).
• Analyze the relationship between a variant's oligomeric state and its corresponding enzymatic activity measurement.
• Validate or compare computational structure predictions from AlphaFold 3 against experimental biochemical data.
• Identify which truncated variants resulted in 'not measured' activity due to experimental issues like large particle flow.

Strengths

• Data is directly linked to 3D protein structures predicted by AlphaFold 3, a state-of-the-art tool.
• Released under a permissive CC-BY-4.0 license, allowing for wide reuse.

Limitations

• The dataset is very small at 5.5 KB, indicating a limited number of protein variants.
• Specific row and column counts are unknown, making the exact data scope unclear.
• Some enzymatic activity values are marked 'not measured', indicating incomplete data points.

Provenance

Source

Figshare, associated with a PLOS Pathogens research article.

Collection Method

Experimental measurement of oligomeric state and enzymatic activity for engineered protein variants.

Freshness

Last updated in April 2026.