Download MendeleyCrystal structure of the Smu1-RED complex (SeMet) of Caenorhabditis elegans
Ulrich, A.K.C., Schulz, J.F., Kamprad, A., Schuetze, T., Wahl, M.C.To be published.
5EN6
Crystal structure of the Smu1-RED complex (SeMet) of Caenorhabditis elegans
- PDB DOI: https://doi.org/10.2210/pdb5EN6/pdb
- Classification: SPLICING
- Organism(s): Caenorhabditis elegans
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): No
- Deposited: 2015-11-09 Released: 2016-04-20
- Funding Organization(s): DFG
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 3.10 Å
- R-Value Free: 0.321
- R-Value Work: 0.283
- R-Value Observed: 0.285
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 |
| SMU-1 | 184 | Caenorhabditis elegans | Mutation(s): 0 Gene Names: smu-1, CC4.3, CELE_CC4.3 |  | |
UniProt | |||||
Find proteins for G5EEG7 (Caenorhabditis elegans) Explore G5EEG7 Go to UniProtKB: G5EEG7 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | G5EEG7 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 2 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| Suppressor of Mec and Unc defects | 63 | Caenorhabditis elegans | Mutation(s): 0 Gene Names: smu-2, CELE_Y49F6B.4, Y49F6B.4 |  | |
UniProt | |||||
Find proteins for Q9N4U5 (Caenorhabditis elegans) Explore Q9N4U5 Go to UniProtKB: Q9N4U5 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q9N4U5 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| 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: 3.10 Å
- R-Value Free: 0.321
- R-Value Work: 0.283
- R-Value Observed: 0.285
- Space Group: C 2 2 21
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 166.669 | α = 90 |
| b = 183.443 | β = 90 |
| c = 41.078 | γ = 90 |
| Software Name | Purpose |
|---|---|
| PHENIX | refinement |
| XSCALE | data scaling |
| SHARP | phasing |
| PDB_EXTRACT | data extraction |
| XDS | data reduction |
Entry History & Funding Information
Deposition Data
- Released Date: 2016-04-20 Deposition Author(s): Ulrich, A.K.C., Wahl, M.C.
| Funding Organization | Location | Grant Number |
|---|---|---|
| DFG | Germany | WA1126/7-1 |
Revision History (Full details and data files)
- Version 1.0: 2016-04-20
Type: Initial release
