X-ray diffraction data for dihydrodipicolinate reductase (DHDPR) from Paenisporosarcina sp. TG-14. The dataset likely contains structural coordinates for the enzyme in unliganded, inhibitor-bound, and cofactor-bound states, supporting a study published in 2017. The data was contributed by the organization AMD_KOPRI.
Use Cases
- Analyzing protein conformational changes based on the described ternary complex structure
- Studying enzyme-cofactor binding interactions based on the NADPH binding site details
- Comparing enzyme kinetics based on the wild-type and mutant forms mentioned
- Investigating structural adaptations of psychrophilic enzymes based on the source organism
Strengths
- Includes high-resolution crystal structures as mentioned in the description
- Contains data for multiple binding states (unliganded, DPA bound, NADPH+DPA bound)
- Supports findings with enzyme kinetics and ITC studies referenced
Limitations
- Row count is unknown, which may limit suitability assessment
- Column-level documentation is absent; field semantics must be inferred after download
- Last updated 2017-10-19 23:59:59.999000; freshness should be verified
Provenance
- Source
- AMD_KOPRI
- Collection Method
- Likely generated via X-ray crystallography and biochemical assays.