AMD_KOPRI provided X-ray diffraction data for a novel cold-active S-formylglutathione hydrolase (SfSFGH) from Shewanella frigidimarina. The dataset likely contains structural and activity analysis results, including a crystal structure determined at 2.32 Å resolution and mutation studies. The data was last updated on July 28, 2017.
Use Cases
- Analyzing enzyme active site configuration based on the crystal structure at 2.32 Å resolution
- Studying substrate specificity changes based on the mutation of Trp182 to Ala
- Evaluating enzyme stability based on activity retention data with various chemicals
- Identifying conserved motifs in lipolytic enzymes based on the G-X-S-X-G pentapeptide sequence
Strengths
- Crystal structure determined at a high resolution of 2.32 Å
- Includes comparative analysis of wild-type and mutant (W182A) enzyme activity
- Provides enzyme stability data with specific chemicals like 30% EtOH, 1% Triton X-100, 1% SDS, and 5 M urea
Limitations
- Description metadata is limited; actual data quality requires manual inspection after download
- Last updated 2017-07-28 23:59:59.999000; freshness should be verified
- Column-level documentation is absent; field semantics must be inferred after download
Provenance
- Source
- AMD_KOPRI