Download MendeleyThe crystal structure of thymidylate kinase from Pseudomonas aeruginosa PAO1 in complex with thymidine monophosphate.
Tan, K., Joachimiak, G., Jedrzejczak, R., Sacchettini, J., Joachimiak, A.To be published.
4E5U
The crystal structure of thymidylate kinase from Pseudomonas aeruginosa PAO1 in complex with thymidine monophosphate.
- PDB DOI: https://doi.org/10.2210/pdb4E5U/pdb
- Classification: TRANSFERASE
- Organism(s): Pseudomonas aeruginosa PAO1
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): No
- Deposited: 2012-03-14 Released: 2012-03-28
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.81 Å
- R-Value Free: 0.231
- R-Value Work: 0.188
- R-Value Observed: 0.191
This is version 1.1 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 |
| Thymidylate kinase | 213 | Pseudomonas aeruginosa PAO1 | Mutation(s): 0 Gene Names: PA2962, tmk EC: 2.7.4.9 |  | |
UniProt | |||||
Find proteins for Q9HZN8 (Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)) Explore Q9HZN8 Go to UniProtKB: Q9HZN8 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q9HZN8 | ||||
Sequence AnnotationsExpand | |||||
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Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| TMP Query on TMP | C [auth A], E [auth B] | THYMIDINE-5'-PHOSPHATE C10 H15 N2 O8 P GYOZYWVXFNDGLU-XLPZGREQSA-N |  | ||
| CA Query on CA | D [auth A], F [auth B], G [auth B] | CALCIUM ION Ca BHPQYMZQTOCNFJ-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: 1.81 Å
- R-Value Free: 0.231
- R-Value Work: 0.188
- R-Value Observed: 0.191
- Space Group: P 21 21 21
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 46.132 | α = 90 |
| b = 57.399 | β = 90 |
| c = 149.952 | γ = 90 |
| Software Name | Purpose |
|---|---|
| SBC-Collect | data collection |
| SHELXD | phasing |
| MLPHARE | phasing |
| DM | model building |
| RESOLVE | model building |
| HKL-3000 | phasing |
| PHENIX | refinement |
| HKL-3000 | data reduction |
| HKL-3000 | data scaling |
| DM | phasing |
| RESOLVE | phasing |
Entry History
Deposition Data
- Released Date: 2012-03-28 Deposition Author(s): Tan, K., Joachimiak, G., Jedrzejczak, R., Sacchettini, J., Joachimiak, A., Midwest Center for Structural Genomics (MCSG), Structures of Mtb Proteins Conferring Susceptibility to Known Mtb Inhibitors (MTBI)
Revision History (Full details and data files)
- Version 1.0: 2012-03-28
Type: Initial release - Version 1.1: 2024-11-27
Changes: Data collection, Database references, Derived calculations, Structure summary
