Download MendeleyCrystal structure of the N-terminal region (19..243) of sensor protein KdpD from Pseudomonas syringae pv. tomato str. DC3000.
Nocek, B., Mulligan, R., Moy, S., Joachimiak, A.To be published.
2R8R
Crystal structure of the N-terminal region (19..243) of sensor protein KdpD from Pseudomonas syringae pv. tomato str. DC3000
- PDB DOI: https://doi.org/10.2210/pdb2R8R/pdb
- Classification: TRANSFERASE
- Organism(s): Pseudomonas syringae pv. tomato str. DC3000
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): No
- Deposited: 2007-09-11 Released: 2007-09-25
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.30 Å
- R-Value Free: 0.216
- R-Value Work: 0.171
- R-Value Observed: 0.173
wwPDB Validation 3D Report Full Report
This is version 1.2 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 |
| Sensor protein | 228 | Pseudomonas syringae pv. tomato str. DC3000 | Mutation(s): 0 Gene Names: kdpD, PSPTO_2245 EC: 2.7.13.3 |  | |
UniProt | |||||
Find proteins for Q883V3 (Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000)) Explore Q883V3 Go to UniProtKB: Q883V3 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q883V3 | ||||
Sequence AnnotationsExpand | |||||
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Small Molecules
| Ligands 3 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| PEG Query on PEG | G [auth A] | DI(HYDROXYETHYL)ETHER C4 H10 O3 MTHSVFCYNBDYFN-UHFFFAOYSA-N |  | ||
| SO4 Query on SO4 | C [auth A], D [auth A], E [auth A], H [auth B], I [auth B] | SULFATE ION O4 S QAOWNCQODCNURD-UHFFFAOYSA-L |  | ||
| GOL Query on GOL | F [auth A], J [auth B] | GLYCEROL C3 H8 O3 PEDCQBHIVMGVHV-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: 2.30 Å
- R-Value Free: 0.216
- R-Value Work: 0.171
- R-Value Observed: 0.173
- Space Group: P 43 21 2
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 56.859 | α = 90 |
| b = 56.859 | β = 90 |
| c = 372.783 | γ = 90 |
| Software Name | Purpose |
|---|---|
| REFMAC | refinement |
| SBC-Collect | data collection |
| HKL-3000 | data reduction |
| HKL-3000 | data scaling |
| HKL2Map | phasing |
| ARP/wARP | model building |
Entry History
Deposition Data
- Released Date: 2007-09-25 Deposition Author(s): Nocek, B., Mulligan, R., Moy, S., Joachimiak, A., Midwest Center for Structural Genomics (MCSG)
Revision History (Full details and data files)
- Version 1.0: 2007-09-25
Type: Initial release - Version 1.1: 2011-07-13
Changes: Advisory, Source and taxonomy, Version format compliance - Version 1.2: 2017-10-25
Changes: Refinement description
