Download MendeleyCrystal structure of glutathione S-transferase from Sinorhizobium meliloti 1021
Shabalin, I.G., Bacal, P., Cooper, D.R., Stead, M., Ahmed, M., Hammonds, J., Bonanno, J., Seidel, R., Almo, S.C., Minor, W.To be published.
4MDC
Crystal structure of glutathione S-transferase from Sinorhizobium meliloti 1021, NYSGRC target 021389
- PDB DOI: https://doi.org/10.2210/pdb4MDC/pdb
- Classification: TRANSFERASE
- Organism(s): Sinorhizobium meliloti 1021
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): No
- Deposited: 2013-08-22 Released: 2013-09-04
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.78 Å
- R-Value Free: 0.190
- R-Value Work: 0.161
- R-Value Observed: 0.163
wwPDB Validation 3D Report Full Report
This is version 1.1 of the entry. See complete history.
Literature
To be published.
Macromolecules
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 1 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| Putative glutathione S-transferase | 252 | Sinorhizobium meliloti 1021 | Mutation(s): 0 Gene Names: gst4, R00327, SMc00407 EC: 2.5.1.18 |  | |
UniProt | |||||
Find proteins for Q92SP3 (Rhizobium meliloti (strain 1021)) Explore Q92SP3 Go to UniProtKB: Q92SP3 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q92SP3 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| GOL Query on GOL | E [auth A], F [auth A], G [auth B] | GLYCEROL C3 H8 O3 PEDCQBHIVMGVHV-UHFFFAOYSA-N |  | ||
| Modified Residues 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Type | Formula | 2D Diagram | Parent |
| MSE Query on MSE | A, B, C, D | L-PEPTIDE LINKING | C5 H11 N O2 Se |  | MET |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.78 Å
- R-Value Free: 0.190
- R-Value Work: 0.161
- R-Value Observed: 0.163
- Space Group: C 1 2 1
- Diffraction Data: https://doi.org/10.18430/m30019
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 182.181 | α = 90 |
| b = 53.508 | β = 115.88 |
| c = 111.123 | γ = 90 |
| Software Name | Purpose |
|---|---|
| SCALEPACK | data scaling |
| SHELX | phasing |
| DM | phasing |
| REFMAC | refinement |
| PDB_EXTRACT | data extraction |
| HKL-3000 | data collection |
| HKL-3000 | data reduction |
| HKL-3000 | data scaling |
| HKL-3000 | phasing |
| SHELXD | phasing |
| MLPHARE | phasing |
| SOLVE | phasing |
| RESOLVE | phasing |
Entry History
Deposition Data
- Released Date: 2013-09-04 Deposition Author(s): Shabalin, I.G., Bacal, P., Cooper, D.R., Stead, M., Ahmed, M., Hammonds, J., Bonanno, J., Seidel, R., Almo, S.C., Minor, W., New York Structural Genomics Research Consortium (NYSGRC)
Revision History (Full details and data files)
- Version 1.0: 2013-09-04
Type: Initial release - Version 1.1: 2022-04-13
Changes: Database references, Derived calculations, Structure summary
