EaEST is a dataset containing X-ray diffraction data for a novel microbial esterase from the psychrophilic bacterium Exiguobacterium antarcticum B7. The crystal structure was determined at a resolution of 1.9 Å, revealing a canonical α/β hydrolase fold and a catalytic triad. The dataset was published by AMD_KOPRI and last updated on April 3, 2016.
Use Cases
- Analyzing enzyme structure based on the 1.9 Å resolution crystal structure
- Studying substrate binding modes based on the peracetate molecule found in the active site
- Comparing conformational changes based on the structural comparison with PfEST (PDB code 3HI4)
- Investigating enzyme activity based on the described perhydrolase and esterase activity assays
- Evaluating enzyme stability based on the immobilized enzyme's retained activity after incubation at 80°C
Strengths
- Crystal structure determined at a high resolution of 1.9 Å
- Includes functional characterization data such as activity assays and enantioselectivity analysis
- Provides structural insights into a novel enzyme from a psychrophilic bacterium
Limitations
- Description metadata is limited; actual data quality requires manual inspection after download
- Last updated 2016-04-03 23:59:59.999000; freshness should be verified
- Column-level documentation is absent; field semantics must be inferred after download
Provenance
- Source
- AMD_KOPRI
- Collection Method
- Likely contains experimental data from X-ray crystallography and biochemical assays.