Download MendeleyC-terminal domain of inner membrane protein CigR from Salmonella enterica.
Osipiuk, J., Xu, X., Cui, H., Brown, R.N., Cort, J.R., Heffron, F., Nakayasu, E.S., Niemann, G.S., Merkley, E.D., Savchenko, A., Adkins, J.N., Joachimiak, A.To be published.
4EW5
C-terminal domain of inner membrane protein CigR from Salmonella enterica.
- PDB DOI: https://doi.org/10.2210/pdb4EW5/pdb
- Classification: MEMBRANE PROTEIN
- Organism(s): Salmonella enterica subsp. enterica serovar Typhimurium str. LT2
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): No
- Deposited: 2012-04-26 Released: 2012-05-23
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.87 Å
- R-Value Free: 0.230
- R-Value Work: 0.176
- R-Value Observed: 0.178
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 |
| CigR Protein | 102 | Salmonella enterica subsp. enterica serovar Typhimurium str. LT2 | Mutation(s): 0 Gene Names: cigR, STM3762 |  | |
UniProt | |||||
Find proteins for Q9Z621 (Salmonella typhimurium) Explore Q9Z621 Go to UniProtKB: Q9Z621 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q9Z621 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| EDO Query on EDO | C [auth A], D [auth B] | 1,2-ETHANEDIOL C2 H6 O2 LYCAIKOWRPUZTN-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: 1.87 Å
- R-Value Free: 0.230
- R-Value Work: 0.176
- R-Value Observed: 0.178
- Space Group: P 21 21 21
- Diffraction Data: https://doi.org/10.18430/M34EW5
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 49.87 | α = 90 |
| b = 54.811 | β = 90 |
| c = 73.992 | γ = 90 |
| Software Name | Purpose |
|---|---|
| DENZO | data reduction |
| SCALEPACK | data scaling |
| REFMAC | refinement |
| PDB_EXTRACT | data extraction |
| SBC-Collect | data collection |
| HKL-3000 | data reduction |
| HKL-3000 | data scaling |
| SHELXD | phasing |
| MLPHARE | phasing |
| DM | phasing |
| ARP/wARP | model building |
| HKL-3000 | phasing |
Entry History
Deposition Data
- Released Date: 2012-05-23 Deposition Author(s): Osipiuk, J., Xu, X., Cui, H., Brown, R.N., Cort, J.R., Heffron, F., Nakayasu, E.S., Niemann, G.S., Merkley, E.D., Savchenko, A., Adkins, J.N., Joachimiak, A., Midwest Center for Structural Genomics (MCSG), Program for the Characterization of Secreted Effector Proteins (PCSEP)
Revision History (Full details and data files)
- Version 1.0: 2012-05-23
Type: Initial release - Version 1.1: 2017-11-15
Changes: Refinement description
