Download MendeleyThe crystal structure of probable glutathione S-transferase from Bordetella bronchiseptica RB50
Tan, K., Xu, X., Cui, H., Savchenko, A., Edwards, A.M., Joachimiak, A.To be published.
3H1N | pdb_00003h1n
Crystal structure of probable glutathione S-transferase from Bordetella bronchiseptica RB50
- PDB DOI: https://doi.org/10.2210/pdb3H1N/pdb
- Classification: TRANSFERASE
- Organism(s): Bordetella bronchiseptica RB50
- Expression System: Escherichia coli
- Mutation(s): No
- Deposited: 2009-04-13 Released: 2009-05-19
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.83 Å
- R-Value Free: 0.223 (Depositor), 0.233 (DCC)
- R-Value Work: 0.184 (Depositor), 0.199 (DCC)
- R-Value Observed: 0.186 (Depositor)
wwPDB Validation 3D Report Full Report
This is version 1.2 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 |
| Probable glutathione S-transferase | 252 | Bordetella bronchiseptica RB50 | Mutation(s): 0 Gene Names: BB0443 |  | |
UniProt | |||||
Find proteins for A0A0H3LPN1 (Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50)) Explore A0A0H3LPN1 Go to UniProtKB: A0A0H3LPN1 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | A0A0H3LPN1 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| EDO Query on EDO | E [auth A], F [auth A] | 1,2-ETHANEDIOL C2 H6 O2 LYCAIKOWRPUZTN-UHFFFAOYSA-N |  | ||
| CL Query on CL | C [auth A] D [auth A] G [auth B] H [auth B] I [auth B] | CHLORIDE ION Cl VEXZGXHMUGYJMC-UHFFFAOYSA-M |  | ||
| Modified Residues 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Type | Formula | 2D Diagram | Parent |
| MSE Query on MSE | A, B | L-PEPTIDE LINKING | C5 H11 N O2 Se |  | MET |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.83 Å
- R-Value Free: 0.223 (Depositor), 0.233 (DCC)
- R-Value Work: 0.184 (Depositor), 0.199 (DCC)
- R-Value Observed: 0.186 (Depositor)
Space Group: P 21 21 21
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 64.949 | α = 90 |
| b = 87.115 | β = 90 |
| c = 91.372 | γ = 90 |
| Software Name | Purpose |
|---|---|
| SBC-Collect | data collection |
| SHELXD | phasing |
| MLPHARE | phasing |
| DM | model building |
| ARP/wARP | model building |
| HKL-3000 | phasing |
| REFMAC | refinement |
| HKL-3000 | data reduction |
| HKL-3000 | data scaling |
| DM | phasing |
Entry History
Deposition Data
- Released Date: 2009-05-19 Deposition Author(s): Tan, K., Xu, X., Cui, H., Savchenko, A., Edwards, A.M., Joachimiak, A., Midwest Center for Structural Genomics (MCSG)
Revision History (Full details and data files)
- Version 1.0: 2009-05-19
Type: Initial release - Version 1.1: 2011-07-13
Changes: Advisory, Version format compliance - Version 1.2: 2024-11-27
Changes: Data collection, Database references, Derived calculations, Structure summary
