Download MendeleyCrystal Structure of the Glutaredoxin 2 from Francisella tularensis
Kim, Y., Zhou, M., Grimshaw, S., Joachimiak, A., Center for Structural Genomics of Infectious Diseases (CSGID)To be published.
7TBS
Crystal Structure of the Glutaredoxin 2 from Francisella tularensis
- PDB DOI: https://doi.org/10.2210/pdb7TBS/pdb
- Classification: TRANSPORT PROTEIN
- Organism(s): Francisella tularensis subsp. tularensis SCHU S4
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): No
- Deposited: 2021-12-22 Released: 2022-01-05
- Funding Organization(s): National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.96 Å
- R-Value Free: 0.217
- R-Value Work: 0.182
- R-Value Observed: 0.184
wwPDB Validation 3D Report Full Report
This is version 1.0 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 2 | 238 | Francisella tularensis subsp. tularensis SCHU S4 | Mutation(s): 0 Gene Names: grxB, FTT_0650c |  | |
UniProt | |||||
Find proteins for Q5NH24 (Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)) Explore Q5NH24 Go to UniProtKB: Q5NH24 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q5NH24 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| SO4 Query on SO4 | B [auth A], C [auth A], D [auth A], E [auth A] | SULFATE ION O4 S QAOWNCQODCNURD-UHFFFAOYSA-L |  | ||
| CL Query on CL | F [auth A] | CHLORIDE ION Cl VEXZGXHMUGYJMC-UHFFFAOYSA-M |  | ||
| Modified Residues 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Type | Formula | 2D Diagram | Parent |
| MSE Query on MSE | A | L-PEPTIDE LINKING | C5 H11 N O2 Se |  | MET |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.96 Å
- R-Value Free: 0.217
- R-Value Work: 0.182
- R-Value Observed: 0.184
- Space Group: I 2 2 2
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 75.989 | α = 90 |
| b = 83.164 | β = 90 |
| c = 84.089 | γ = 90 |
| Software Name | Purpose |
|---|---|
| PHENIX | refinement |
| HKL-3000 | data reduction |
| HKL-3000 | data scaling |
| HKL-3000 | phasing |
| MLPHARE | phasing |
Entry History & Funding Information
Deposition Data
- Released Date: 2022-01-05 Deposition Author(s): Kim, Y., Zhou, M., Grimshaw, S., Joachimiak, A., Center for Structural Genomics of Infectious Diseases (CSGID)
| Funding Organization | Location | Grant Number |
|---|---|---|
| National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID) | United States | -- |
Revision History (Full details and data files)
- Version 1.0: 2022-01-05
Type: Initial release
