Download MendeleyThe crystal structure of glycyl-tRNA synthetase subunit alpha from Campylobacter jejuni subsp. jejuni NCTC 11168
Tan, K., Zhang, R., Zhou, M., Hasseman, J., Anderson, W.F., Joachimiak, A.To be published.
3RF1
The crystal structure of glycyl-tRNA synthetase subunit alpha from Campylobacter jejuni subsp. jejuni NCTC 11168
- PDB DOI: https://doi.org/10.2210/pdb3RF1/pdb
- Classification: LIGASE
- Organism(s): Campylobacter jejuni subsp. jejuni 81-176
- Expression System: Escherichia coli
- Mutation(s): No
- Deposited: 2011-04-05 Released: 2011-04-20
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.20 Å
- R-Value Free: 0.214
- R-Value Work: 0.169
- R-Value Observed: 0.172
wwPDB Validation 3D Report Full Report
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 |
| Glycyl-tRNA synthetase alpha subunit | 311 | Campylobacter jejuni subsp. jejuni 81-176 | Mutation(s): 0 Gene Names: glyQ, CJJ81176_0727 EC: 6.1.1.14 |  | |
UniProt | |||||
Find proteins for A1VZ59 (Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176)) Explore A1VZ59 Go to UniProtKB: A1VZ59 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | A1VZ59 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| LMR Query on LMR | C [auth A], E [auth B] | (2S)-2-hydroxybutanedioic acid C4 H6 O5 BJEPYKJPYRNKOW-REOHCLBHSA-N |  | ||
| GOL Query on GOL | D [auth A], F [auth B], G [auth B], H [auth B], I [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: 2.20 Å
- R-Value Free: 0.214
- R-Value Work: 0.169
- R-Value Observed: 0.172
- Space Group: H 3
- Diffraction Data: https://doi.org/10.18430/M33RF1
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 112.662 | α = 90 |
| b = 112.662 | β = 90 |
| c = 158.282 | γ = 120 |
| Software Name | Purpose |
|---|---|
| SBC-Collect | data collection |
| MOLREP | phasing |
| PHENIX | refinement |
| HKL-3000 | data reduction |
| HKL-3000 | data scaling |
Entry History
Deposition Data
- Released Date: 2011-04-20 Deposition Author(s): Tan, K., Zhang, R., Zhou, M., Hasseman, J., Anderson, W.F., Joachimiak, A., Center for Structural Genomics of Infectious Diseases (CSGID)
Revision History (Full details and data files)
- Version 1.0: 2011-04-20
Type: Initial release - Version 1.1: 2011-07-13
Changes: Version format compliance - Version 1.2: 2023-09-13
Changes: Data collection, Database references, Derived calculations, Refinement description - Version 1.3: 2023-12-06
Changes: Data collection
