Download MendeleyCrystal structure of UPF0341 protein yhiQ from Salmonella typhimurium.
Forouhar, F., Su, M., Seetharaman, J., Fang, Y., Xiao, R., Cunningham, K., Ma, L.-C., Owens, L., Liu, J., Acton, T.B., Montelione, G.T., Tong, L., Hunt, J.F.To be published.
2PKW
Crystal structure of UPF0341 protein yhiQ from Salmonella typhimurium, Northeast Structural Genomics Consortium Target StR221
- PDB DOI: https://doi.org/10.2210/pdb2PKW/pdb
- Classification: STRUCTURAL GENOMICS, UNKNOWN FUNCTION
- Organism(s): Salmonella enterica subsp. enterica serovar Typhimurium str. LT2
- Expression System: Escherichia coli
- Mutation(s): Yes
- Deposited: 2007-04-18 Released: 2007-05-01
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.10 Å
- R-Value Free: 0.259
- R-Value Work: 0.208
- R-Value Observed: 0.208
wwPDB Validation 3D Report Full Report
This is version 1.4 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 |
| UPF0341 protein yhiQ | 260 | Salmonella enterica subsp. enterica serovar Typhimurium str. LT2 | Mutation(s): 8 Gene Names: yhiQ, STM3593 |  | |
UniProt | |||||
Find proteins for Q9X6G2 (Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)) Explore Q9X6G2 Go to UniProtKB: Q9X6G2 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q9X6G2 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| TRS Query on TRS | B [auth A] | 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL C4 H12 N O3 LENZDBCJOHFCAS-UHFFFAOYSA-O |  | ||
| Modified Residues 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Type | Formula | 2D Diagram | Parent |
| MSE Query on MSE | A | L-PEPTIDE LINKING | C5 H11 N O2 Se |  | MET |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 2.10 Å
- R-Value Free: 0.259
- R-Value Work: 0.208
- R-Value Observed: 0.208
- Space Group: P 21 21 21
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 41.967 | α = 90 |
| b = 70.248 | β = 90 |
| c = 77.788 | γ = 90 |
| Software Name | Purpose |
|---|---|
| CNS | refinement |
| ADSC | data collection |
| HKL-2000 | data reduction |
| SCALEPACK | data scaling |
| SnB | phasing |
| RESOLVE | phasing |
Entry History
Deposition Data
- Released Date: 2007-05-01 Deposition Author(s): Forouhar, F., Su, M., Seetharaman, J., Fang, Y., Xiao, R., Cunningham, K., Ma, L.-C., Owens, L., Liu, J., Acton, T.B., Montelione, G.T., Tong, L., Hunt, J.F., Northeast Structural Genomics Consortium (NESG)
Revision History (Full details and data files)
- Version 1.0: 2007-05-01
Type: Initial release - Version 1.1: 2008-05-01
Changes: Version format compliance - Version 1.2: 2011-07-13
Changes: Version format compliance - Version 1.3: 2017-10-18
Changes: Refinement description - Version 1.4: 2018-01-24
Changes: Database references, Structure summary
