Download MendeleyCrystal structure of Putative sugar binding protein (NP_459565.1) from Salmonella typhimurium LT2 at 2.50 A resolution
Joint Center for Structural Genomics (JCSG)To be published.
3KNZ
Crystal structure of Putative sugar binding protein (NP_459565.1) from Salmonella typhimurium LT2 at 2.50 A resolution
- PDB DOI: https://doi.org/10.2210/pdb3KNZ/pdb
- Classification: SUGAR BINDING PROTEIN
- Organism(s): Salmonella enterica subsp. enterica serovar Typhimurium
- Expression System: Escherichia coli
- Mutation(s): No
- Deposited: 2009-11-12 Released: 2009-12-01
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.50 Å
- R-Value Free: 0.232
- R-Value Work: 0.203
- R-Value Observed: 0.205
wwPDB Validation 3D Report Full Report
This is version 1.3 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 |
| Putative sugar binding protein | 366 | Salmonella enterica subsp. enterica serovar Typhimurium | Mutation(s): 0 Gene Names: STM0573 |  | |
UniProt | |||||
Find proteins for Q8ZR49 (Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)) Explore Q8ZR49 Go to UniProtKB: Q8ZR49 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q8ZR49 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| ETX Query on ETX | G [auth A], J [auth D] | 2-ETHOXYETHANOL C4 H10 O2 ZNQVEEAIQZEUHB-UHFFFAOYSA-N |  | ||
| IMD Query on IMD | H [auth A], I [auth C] | IMIDAZOLE C3 H5 N2 RAXXELZNTBOGNW-UHFFFAOYSA-O |  | ||
| Modified Residues 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Type | Formula | 2D Diagram | Parent |
| MSE Query on MSE | A, B, C, D, E A, B, C, D, E, F | L-PEPTIDE LINKING | C5 H11 N O2 Se |  | MET |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 2.50 Å
- R-Value Free: 0.232
- R-Value Work: 0.203
- R-Value Observed: 0.205
- Space Group: P 21 21 21
- Diffraction Data: https://doi.org/10.18430/M33KNZ
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 90.028 | α = 90 |
| b = 173.344 | β = 90 |
| c = 208.574 | γ = 90 |
| Software Name | Purpose |
|---|---|
| REFMAC | refinement |
| PHENIX | refinement |
| SOLVE | phasing |
| MolProbity | model building |
| SCALA | data scaling |
| PDB_EXTRACT | data extraction |
| MOSFLM | data reduction |
Entry History
Deposition Data
- Released Date: 2009-12-01 Deposition Author(s): Joint Center for Structural Genomics (JCSG)
Revision History (Full details and data files)
- Version 1.0: 2009-12-01
Type: Initial release - Version 1.1: 2011-07-13
Changes: Advisory, Version format compliance - Version 1.2: 2017-10-25
Changes: Author supporting evidence, Refinement description - Version 1.3: 2019-07-17
Changes: Data collection, Derived calculations, Refinement description
