The x-ray crystal structure of succinyl-CoA synthetase from Escherichia coli has been determined to a resolution of 2.5 Angstroms. The model has been refined to a conventional R factor of 21.6% with root mean square deviations from ideal stereochemistry of 0.022 A for bond lengths and 3.25 degrees for bond angles. The structure was determined by William T. Wolodko of the University of Alberta.
Use Cases
- Analyzing enzyme active site geometry based on the described location at regions of contact between alpha- and beta-subunits.
- Studying protein quaternary organization based on the described alpha 2 beta 2 heterotetramer structure.
- Modeling cofactor binding interactions based on the described binding of coenzyme A to each alpha-subunit.
- Investigating catalytic intermediate stabilization based on the described phosphohistidine stabilized by two helix dipoles.
Strengths
- High-resolution structural data at 2.5 Angstroms.
- Refined model with a conventional R factor of 21.6% and specific stereochemistry metrics (0.022 A bond lengths, 3.25 degrees bond angles).
- Detailed description of quaternary organization and active site pockets.
Limitations
- Column-level documentation is absent; field semantics must be inferred after download.
- Row count is unknown, which may limit suitability assessment.
- Last update date is unknown; freshness unverified.
Provenance
- Source
- William T. Wolodko, University of Alberta
- Collection Method
- X-ray crystallography using the method of multiple isomorphous replacement.