Download Mendeley2.7 Angstrom resolution structure of 3-phosphoshikimate 1-carboxyvinyltransferase (AroA) from Coxiella burnetii in second conformational state
Light, S.H., Minasov, G., Krishna, S.N., Shuvalova, L., Papazisi, L., Anderson, W.F.To be published.
4GFP
2.7 Angstrom resolution structure of 3-phosphoshikimate 1-carboxyvinyltransferase (AroA) from Coxiella burnetii in a second conformational state
- PDB DOI: https://doi.org/10.2210/pdb4GFP/pdb
- Classification: TRANSFERASE
- Organism(s): Coxiella burnetii RSA 493
- Expression System: Escherichia coli BL21
- Mutation(s): No
- Deposited: 2012-08-03 Released: 2012-08-15
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.70 Å
- R-Value Free: 0.261
- R-Value Work: 0.227
- R-Value Observed: 0.229
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 |
| 3-phosphoshikimate 1-carboxyvinyltransferase | 462 | Coxiella burnetii RSA 493 | Mutation(s): 0 Gene Names: aroA, CBU_0526 EC: 2.5.1.19 |  | |
UniProt | |||||
Find proteins for Q83E11 (Coxiella burnetii (strain RSA 493 / Nine Mile phase I)) Explore Q83E11 Go to UniProtKB: Q83E11 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q83E11 | ||||
Sequence AnnotationsExpand | |||||
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Small Molecules
| Ligands 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| BME Query on BME | B [auth A], C [auth A] | BETA-MERCAPTOETHANOL C2 H6 O S DGVVWUTYPXICAM-UHFFFAOYSA-N |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 2.70 Å
- R-Value Free: 0.261
- R-Value Work: 0.227
- R-Value Observed: 0.229
- Space Group: P 64
- Diffraction Data: https://doi.org/10.18430/m34gfp
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 125.426 | α = 90 |
| b = 125.426 | β = 90 |
| c = 108.26 | γ = 120 |
| Software Name | Purpose |
|---|---|
| HKL-2000 | data collection |
| PHASER | phasing |
| REFMAC | refinement |
| HKL-3000 | data reduction |
| HKL-3000 | data scaling |
Entry History
Deposition Data
- Released Date: 2012-08-15 Deposition Author(s): Light, S.H., Minasov, G., Krishna, S.N., Shuvalova, L., Papazisi, L., Anderson, W.F., Center for Structural Genomics of Infectious Diseases (CSGID)
Revision History (Full details and data files)
- Version 1.0: 2012-08-15
Type: Initial release - Version 1.1: 2023-09-13
Changes: Data collection, Database references, Derived calculations, Refinement description
