Download MendeleyThe Structure of the Insc:Lgn Tetramer Reveals a New Function of Lgn in Promoting Asymmetric Cell Divisions
Culurgioni, S., Mari, S., Bonetto, G., Gallini, S., Brennich, M., Round, A., Mapelli, M.To be published.
5A7D | pdb_00005a7d
Tetrameric assembly of LGN with Inscuteable
- PDB DOI: https://doi.org/10.2210/pdb5A7D/pdb
- Classification: CELL CYCLE
- Organism(s): Drosophila melanogaster
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): No
- Deposited: 2015-07-07 Released: 2016-08-03
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 3.40 Å
- R-Value Free: 0.250 (Depositor), 0.250 (DCC)
- R-Value Work: 0.209 (Depositor), 0.210 (DCC)
- R-Value Observed: 0.211 (Depositor)
Starting Model: experimental
View more details
wwPDB Validation 3D Report Full Report
This is version 1.2 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 |
| PINS | 382 | Drosophila melanogaster | Mutation(s): 0 |  | |
UniProt | |||||
Find proteins for Q9VB22 (Drosophila melanogaster) Explore Q9VB22 Go to UniProtKB: Q9VB22 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q9VB22 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 2 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| INSCUTEABLE | 341 | Drosophila melanogaster | Mutation(s): 0 |  | |
UniProt | |||||
Find proteins for Q24367 (Drosophila melanogaster) Explore Q24367 Go to UniProtKB: Q24367 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q24367 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 3.40 Å
- R-Value Free: 0.250 (Depositor), 0.250 (DCC)
- R-Value Work: 0.209 (Depositor), 0.210 (DCC)
- R-Value Observed: 0.211 (Depositor)
Space Group: P 21 21 21
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 128.19 | α = 90 |
| b = 212.58 | β = 90 |
| c = 280.73 | γ = 90 |
| Software Name | Purpose |
|---|---|
| PHENIX | refinement |
| XDS | data reduction |
| SCALA | data scaling |
| PHASER | phasing |
Entry History
Deposition Data
- Released Date: 2016-08-03 Deposition Author(s): Culurgioni, S., Mari, S., Bonetto, G., Gallini, S., Brennich, M., Round, A., Mapelli, M.
Revision History (Full details and data files)
- Version 1.0: 2016-08-03
Type: Initial release - Version 1.1: 2018-05-23
Changes: Data collection, Derived calculations - Version 1.2: 2024-01-10
Changes: Data collection, Database references, Other, Refinement description
