Download MendeleyThe crystal structure of a flagella protein from Yersinia enterocolitica subsp. enterocolitica 8081
Tan, K., Li, H., Feldmann, B., Joachimiak, A.To be published.
3NKZ
The crystal structure of a flagella protein from Yersinia enterocolitica subsp. enterocolitica 8081
- PDB DOI: https://doi.org/10.2210/pdb3NKZ/pdb
- Classification: structural genomics, unknown function
- Organism(s): Yersinia enterocolitica subsp. enterocolitica 8081
- Expression System: Escherichia coli
- Mutation(s): No
- Deposited: 2010-06-21 Released: 2010-08-18
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.11 Å
- R-Value Free: 0.192
- R-Value Work: 0.159
- R-Value Observed: 0.158
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 |
| Flagellar protein fliT | 123 | Yersinia enterocolitica subsp. enterocolitica 8081 | Mutation(s): 0 Gene Names: fliT, YE2526 |  | |
UniProt | |||||
Find proteins for A1JSR8 (Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 / 8081)) Explore A1JSR8 Go to UniProtKB: A1JSR8 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | A1JSR8 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| PG4 Query on PG4 | F [auth A], I [auth C] | TETRAETHYLENE GLYCOL C8 H18 O5 UWHCKJMYHZGTIT-UHFFFAOYSA-N |  | ||
| SO4 Query on SO4 | E [auth A], G [auth B], H [auth C], J [auth D] | SULFATE ION O4 S QAOWNCQODCNURD-UHFFFAOYSA-L |  | ||
| Modified Residues 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Type | Formula | 2D Diagram | Parent |
| MSE Query on MSE | A, B, C, D | L-PEPTIDE LINKING | C5 H11 N O2 Se |  | MET |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 2.11 Å
- R-Value Free: 0.192
- R-Value Work: 0.159
- R-Value Observed: 0.158
- Space Group: P 21 21 21
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 66.798 | α = 90 |
| b = 66.758 | β = 90 |
| c = 137.649 | γ = 90 |
| Software Name | Purpose |
|---|---|
| SBC-Collect | data collection |
| SHELXD | phasing |
| MLPHARE | phasing |
| DM | model building |
| RESOLVE | model building |
| HKL-3000 | phasing |
| PHENIX | refinement |
| HKL-3000 | data reduction |
| HKL-3000 | data scaling |
| DM | phasing |
| RESOLVE | phasing |
Entry History
Deposition Data
- Released Date: 2010-08-18 Deposition Author(s): Tan, K., Li, H., Feldmann, B., Joachimiak, A., Midwest Center for Structural Genomics (MCSG)
Revision History (Full details and data files)
- Version 1.0: 2010-08-18
Type: Initial release - Version 1.1: 2011-07-13
Changes: Version format compliance
