Download MendeleyCrystal Structure of Glutaredoxin 1 from Francisella tularensis Complexed with Cacodylate
Maltseva, N., Kim, Y., Kwon, K., Anderson, W.F., Joachimiak, A.To be published.
3MSZ
Crystal Structure of Glutaredoxin 1 from Francisella tularensis Complexed with Cacodylate
- PDB DOI: https://doi.org/10.2210/pdb3MSZ/pdb
- Classification: OXIDOREDUCTASE
- Organism(s): Francisella tularensis subsp. tularensis SCHU S4
- Expression System: Escherichia coli
- Mutation(s): No
- Deposited: 2010-04-29 Released: 2010-05-19
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.05 Å
- R-Value Free: 0.223
- R-Value Work: 0.173
- R-Value Observed: 0.175
This is version 1.3 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 |
| Glutaredoxin 1 | 89 | Francisella tularensis subsp. tularensis SCHU S4 | Mutation(s): 0 Gene Names: FTT_0533c, grxA |  | |
UniProt | |||||
Find proteins for Q5NHD0 (Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)) Explore Q5NHD0 Go to UniProtKB: Q5NHD0 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q5NHD0 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 3 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| GSH Query on GSH | D [auth A], E [auth B] | GLUTATHIONE C10 H17 N3 O6 S RWSXRVCMGQZWBV-WDSKDSINSA-N |  | ||
| CAC Query on CAC | C [auth A] | CACODYLATE ION C2 H6 As O2 OGGXGZAMXPVRFZ-UHFFFAOYSA-M |  | ||
| GOL Query on GOL | F [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 | L-PEPTIDE LINKING | C5 H11 N O2 Se |  | MET |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 2.05 Å
- R-Value Free: 0.223
- R-Value Work: 0.173
- R-Value Observed: 0.175
- Space Group: P 32 2 1
- Diffraction Data: https://doi.org/10.18430/M33MSZ
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 49.139 | α = 90 |
| b = 49.139 | β = 90 |
| c = 140.199 | γ = 120 |
| Software Name | Purpose |
|---|---|
| SBC-Collect | data collection |
| HKL-3000 | data collection |
| BALBES | phasing |
| PHENIX | refinement |
| HKL-3000 | data reduction |
| HKL-3000 | data scaling |
Entry History
Deposition Data
- Released Date: 2010-05-19 Deposition Author(s): Maltseva, N., Kim, Y., Kwon, K., Anderson, W.F., Joachimiak, A., Center for Structural Genomics of Infectious Diseases (CSGID)
Revision History (Full details and data files)
- Version 1.0: 2010-05-19
Type: Initial release - Version 1.1: 2011-07-13
Changes: Version format compliance - Version 1.2: 2023-09-06
Changes: Data collection, Database references, Derived calculations, Refinement description - Version 1.3: 2023-11-22
Changes: Data collection
