Download MendeleyX-ray crystal structure of C-terminal domain of putative thiol-disulfide oxidoreductase from Bacteroides thetaiotaomicron.
Osipiuk, J., Li, H., Cobb, G., Joachimiak, A.To be published.
3FW2
C-terminal domain of putative thiol-disulfide oxidoreductase from Bacteroides thetaiotaomicron.
- PDB DOI: https://doi.org/10.2210/pdb3FW2/pdb
- Classification: OXIDOREDUCTASE
- Organism(s): Bacteroides thetaiotaomicron
- Expression System: Escherichia coli
- Mutation(s): No
- Deposited: 2009-01-16 Released: 2009-01-27
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.74 Å
- R-Value Free: 0.204
- R-Value Work: 0.164
- R-Value Observed: 0.166
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 |
| thiol-disulfide oxidoreductase | 150 | Bacteroides thetaiotaomicron | Mutation(s): 0 Gene Names: BT_2845 |  | |
UniProt | |||||
Find proteins for Q8A3V9 (Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / VPI-5482 / E50)) Explore Q8A3V9 Go to UniProtKB: Q8A3V9 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q8A3V9 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| EDO Query on EDO | H [auth C] | 1,2-ETHANEDIOL C2 H6 O2 LYCAIKOWRPUZTN-UHFFFAOYSA-N |  | ||
| ACT Query on ACT | E [auth A], F [auth A], G [auth B], I [auth D] | ACETATE ION C2 H3 O2 QTBSBXVTEAMEQO-UHFFFAOYSA-M |  | ||
| 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: 1.74 Å
- R-Value Free: 0.204
- R-Value Work: 0.164
- R-Value Observed: 0.166
- Space Group: P 21 21 21
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 63.441 | α = 90 |
| b = 96.704 | β = 90 |
| c = 116.489 | γ = 90 |
| Software Name | Purpose |
|---|---|
| DENZO | data reduction |
| SCALEPACK | data scaling |
| REFMAC | refinement |
| PDB_EXTRACT | data extraction |
| SBC-Collect | data collection |
| HKL-3000 | data reduction |
| SHELXD | phasing |
| MLPHARE | phasing |
| DM | phasing |
| SOLVE | phasing |
| RESOLVE | phasing |
| HKL-3000 | phasing |
Entry History
Deposition Data
- Released Date: 2009-01-27 Deposition Author(s): Osipiuk, J., Li, H., Cobb, G., Joachimiak, A., Midwest Center for Structural Genomics (MCSG)
Revision History (Full details and data files)
- Version 1.0: 2009-01-27
Type: Initial release - Version 1.1: 2011-07-13
Changes: Advisory, Version format compliance - Version 1.2: 2017-11-01
Changes: Refinement description
