Download MendeleyThe crystal structure of PHOSPHOENOLPYRUVATE PHOSPHOMUTASE from Streptomyces platensis subsp. rosaceus
Tan, K., Hatzos-Skintges, C., Endres, M., Phillips Jr., G.N., Joachimiak, A.To be published.
5UNC
The crystal structure of PHOSPHOENOLPYRUVATE PHOSPHOMUTASE from Streptomyces platensis subsp. rosaceus
- PDB DOI: https://doi.org/10.2210/pdb5UNC/pdb
- Classification: ISOMERASE
- Organism(s): Streptomyces platensis
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): No
- Deposited: 2017-01-30 Released: 2017-02-22
- Funding Organization(s): National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.71 Å
- R-Value Free: 0.177
- R-Value Work: 0.155
- R-Value Observed: 0.156
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 |
| PHOSPHOENOLPYRUVATE PHOSPHOMUTASE | 337 | Streptomyces platensis | Mutation(s): 0 |  | |
UniProt | |||||
Find proteins for A0A0A0V023 (Streptomyces platensis) Explore A0A0A0V023 Go to UniProtKB: A0A0A0V023 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | A0A0A0V023 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 3 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| XYS Query on XYS | F [auth A], G [auth A], M [auth C], O [auth D] | alpha-D-xylopyranose C5 H10 O5 SRBFZHDQGSBBOR-LECHCGJUSA-N |  | ||
| TLA Query on TLA | E [auth A], H [auth B], J [auth C], K [auth C], N [auth D] | L(+)-TARTARIC ACID C4 H6 O6 FEWJPZIEWOKRBE-JCYAYHJZSA-N |  | ||
| FMT Query on FMT | I [auth B], L [auth C] | FORMIC ACID C H2 O2 BDAGIHXWWSANSR-UHFFFAOYSA-N |  | ||
| 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: 1.71 Å
- R-Value Free: 0.177
- R-Value Work: 0.155
- R-Value Observed: 0.156
- Space Group: P 21 21 21
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 89.326 | α = 90 |
| b = 122.036 | β = 90 |
| c = 136.681 | γ = 90 |
| Software Name | Purpose |
|---|---|
| PHENIX | refinement |
| HKL-3000 | data reduction |
| HKL-3000 | data scaling |
| HKL-3000 | phasing |
Entry History & Funding Information
Deposition Data
- Released Date: 2017-02-22 Deposition Author(s): Tan, K., Hatzos-Skintges, C., Endres, M., Phillips Jr., G.N., Joachimiak, A., Midwest Center for Structural Genomics (MCSG), Enzyme Discovery for Natural Product Biosynthesis (NatPro)
| Funding Organization | Location | Grant Number |
|---|---|---|
| National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS) | United States | GM115586 |
Revision History (Full details and data files)
- Version 1.0: 2017-02-22
Type: Initial release - Version 1.1: 2017-09-20
Changes: Author supporting evidence - Version 1.2: 2020-01-01
Changes: Author supporting evidence, Data collection - Version 1.3: 2020-07-29
Type: Remediation
Reason: Carbohydrate remediation
Changes: Data collection, Derived calculations, Structure summary
