Download MendeleyThe crystal structure of a possible phosphate binding protein from Planctomyces limnophilus DSM 3776
Tan, K., Gu, M., Endres, M., Joachimiak, A.To be published.
4JWO
The crystal structure of a possible phosphate binding protein from Planctomyces limnophilus DSM 3776
- PDB DOI: https://doi.org/10.2210/pdb4JWO/pdb
- Classification: Phosphate binding protein
- Organism(s): Planctopirus limnophila DSM 3776
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): No
- Deposited: 2013-03-27 Released: 2013-04-24
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.60 Å
- R-Value Free: 0.195
- R-Value Work: 0.172
- R-Value Observed: 0.173
wwPDB Validation 3D Report Full Report
This is version 1.0 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 |
| Phosphate binding protein | 341 | Planctopirus limnophila DSM 3776 | Mutation(s): 0 Gene Names: Plim_1490 |  | |
UniProt | |||||
Find proteins for D5SW38 (Planctopirus limnophila (strain ATCC 43296 / DSM 3776 / IFAM 1008 / Mu 290)) Explore D5SW38 Go to UniProtKB: D5SW38 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | D5SW38 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 4 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| PEG Query on PEG | F [auth A], G [auth A] | DI(HYDROXYETHYL)ETHER C4 H10 O3 MTHSVFCYNBDYFN-UHFFFAOYSA-N |  | ||
| SO4 Query on SO4 | B [auth A], C [auth A], D [auth A] | SULFATE ION O4 S QAOWNCQODCNURD-UHFFFAOYSA-L |  | ||
| EDO Query on EDO | H [auth A] | 1,2-ETHANEDIOL C2 H6 O2 LYCAIKOWRPUZTN-UHFFFAOYSA-N |  | ||
| FMT Query on FMT | E [auth A] | FORMIC ACID C H2 O2 BDAGIHXWWSANSR-UHFFFAOYSA-N |  | ||
| 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: 1.60 Å
- R-Value Free: 0.195
- R-Value Work: 0.172
- R-Value Observed: 0.173
- Space Group: P 61
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 87.158 | α = 90 |
| b = 87.158 | β = 90 |
| c = 75.536 | γ = 120 |
| Software Name | Purpose |
|---|---|
| SBC-Collect | data collection |
| SHELXD | phasing |
| MLPHARE | phasing |
| DM | model building |
| ARP | model building |
| WARP | model building |
| HKL-3000 | phasing |
| PHENIX | refinement |
| HKL-3000 | data reduction |
| HKL-3000 | data scaling |
| DM | phasing |
Entry History
Deposition Data
- Released Date: 2013-04-24 Deposition Author(s): Tan, K., Gu, M., Endres, M., Joachimiak, A., Midwest Center for Structural Genomics (MCSG)
Revision History (Full details and data files)
- Version 1.0: 2013-04-24
Type: Initial release
