Download MendeleyCrystal structure of a phosphoserine phosphohydrolase-like protein from Francisella tularensis subsp. tularensis SCHUS4
Nocek, B., Zhou, M., Peterson, S., Anderson, W., Joachimiak, A., CSGIDTo be published.
3KD3
Crystal structure of a phosphoserine phosphohydrolase-like protein from Francisella tularensis subsp. tularensis SCHU S4
- PDB DOI: https://doi.org/10.2210/pdb3KD3/pdb
- Classification: UNKNOWN FUNCTION
- Organism(s): Francisella tularensis subsp. tularensis
- Expression System: Escherichia coli
- Mutation(s): No
- Deposited: 2009-10-22 Released: 2009-12-15
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.70 Å
- R-Value Free: 0.186
- R-Value Work: 0.163
- R-Value Observed: 0.164
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 |
| Phosphoserine phosphohydrolase-like protein | 219 | Francisella tularensis subsp. tularensis | Mutation(s): 0 Gene Names: FTT0568, FTT_0568 |  | |
UniProt | |||||
Find proteins for Q5NH99 (Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)) Explore Q5NH99 Go to UniProtKB: Q5NH99 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q5NH99 | ||||
Sequence AnnotationsExpand | |||||
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Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| GOL Query on GOL | D [auth A], E [auth A], G [auth B] | GLYCEROL C3 H8 O3 PEDCQBHIVMGVHV-UHFFFAOYSA-N |  | ||
| MG Query on MG | C [auth A], F [auth B] | MAGNESIUM ION Mg JLVVSXFLKOJNIY-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: 1.70 Å
- R-Value Free: 0.186
- R-Value Work: 0.163
- R-Value Observed: 0.164
- Space Group: P 21 21 21
- Diffraction Data: https://doi.org/10.18430/M33KD3
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 72.574 | α = 90 |
| b = 78.798 | β = 90 |
| c = 87.918 | γ = 90 |
| Software Name | Purpose |
|---|---|
| SBC-Collect | data collection |
| HKL-3000 | phasing |
| REFMAC | refinement |
| HKL-3000 | data reduction |
| HKL-3000 | data scaling |
Entry History
Deposition Data
- Released Date: 2009-12-15 Deposition Author(s): Nocek, B., Zhou, M., Peterson, S., Anderson, W., Joachimiak, A., CSGID, Center for Structural Genomics of Infectious Diseases (CSGID)
Revision History (Full details and data files)
- Version 1.0: 2009-12-15
Type: Initial release - Version 1.1: 2011-07-13
Changes: Advisory, Version format compliance - Version 1.2: 2017-02-08
Changes: Database references, Structure summary - Version 1.3: 2018-01-24
Changes: Structure summary
