Download MendeleyPhenylalanyl-tRNA Synthetase Domain Swap: evolutionary advantage?
Real-Hohn, A., Ross, J.J., Stefania, V., Burga, A., Dong, G.To be published.
8S8B | pdb_00008s8b
Phenylalanyl-tRNA Synthetase Domain Swap: evolutionary advantage?
- PDB DOI: https://doi.org/10.2210/pdb8S8B/pdb
- EM Map EMD-19800: EMDB EMDataResource
- Classification: RNA BINDING PROTEIN
- Organism(s): Caenorhabditis tropicalis
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): No
- Deposited: 2024-03-06 Released: 2025-03-19
- Funding Organization(s): Austrian Science Fund
Experimental Data Snapshot
- Method: ELECTRON MICROSCOPY
- Resolution: 2.80 Å
- Aggregation State: PARTICLE
- Reconstruction Method: SINGLE PARTICLE
Starting Model: in silico
View more details
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 |
| Phenylalanyl-tRNA Synthetase alpha subunit | 496 | Caenorhabditis tropicalis | Mutation(s): 0 EC: 6.1.1.20 |  | |
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
Sequence AnnotationsExpand | |||||
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Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 2 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| Phenylalanyl-tRNA Synthetase beta subunit | 590 | Caenorhabditis tropicalis | Mutation(s): 0 EC: 6.1.1.20 |  | |
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| MG (Subject of Investigation/LOI) Query on MG | E [auth A], F [auth B] | MAGNESIUM ION Mg JLVVSXFLKOJNIY-UHFFFAOYSA-N |  | ||
Experimental Data & Validation
Experimental Data
- Method: ELECTRON MICROSCOPY
- Resolution: 2.80 Å
- Aggregation State: PARTICLE
- Reconstruction Method: SINGLE PARTICLE
Entry History & Funding Information
Deposition Data
- Released Date: 2025-03-19 Deposition Author(s): Real-Hohn, A., Ross, J.J., Stefania, V., Burga, A., Dong, G.
| Funding Organization | Location | Grant Number |
|---|---|---|
| Austrian Science Fund | Austria | P34880 |
Revision History (Full details and data files)
- Version 1.0: 2025-03-19
Type: Initial release
