Download MendeleyCrystal structure of the uridine phosphorylase from Salmonella typhimurium in complex with inhibitor and phosphate ion at 1.85A resolution
Gabdoulkhakov, A.G., Dontsova, M.V., Lashkov, A.A., Betzel, C., Ealick, S., Mikhailov, A.M.To be published.
1ZL2
Crystal structure of the uridine phosphorylase from Salmonella typhimurium in complex with 2,2'-anhydrouridine and phosphate ion at 1.85A resolution
- PDB DOI: https://doi.org/10.2210/pdb1ZL2/pdb
- Classification: TRANSFERASE
- Organism(s): Salmonella enterica subsp. enterica serovar Typhimurium str. LT2
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): No
- Deposited: 2005-05-05 Released: 2006-05-09
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.85 Å
- R-Value Free: 0.198
- R-Value Work: 0.178
- R-Value Observed: 0.178
Starting Model: experimental
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This is version 1.5 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 |
| Uridine phosphorylase | 253 | Salmonella enterica subsp. enterica serovar Typhimurium str. LT2 | Mutation(s): 0 Gene Names: UDP EC: 2.4.2.3 |  | |
UniProt | |||||
Find proteins for P0A1F6 (Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)) Explore P0A1F6 Go to UniProtKB: P0A1F6 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | P0A1F6 | ||||
Sequence AnnotationsExpand | |||||
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Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| ANU Query on ANU | H [auth B], J [auth D], L [auth F] | 2,2'-Anhydro-(1-beta-D-arabinofuranosyl)uracil C9 H10 N2 O5 UUGITDASWNOAGG-CCXZUQQUSA-N |  | ||
| PO4 Query on PO4 | G [auth B], I [auth D], K [auth F] | PHOSPHATE ION O4 P NBIIXXVUZAFLBC-UHFFFAOYSA-K |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.85 Å
- R-Value Free: 0.198
- R-Value Work: 0.178
- R-Value Observed: 0.178
- Space Group: P 21 21 21
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 88.79 | α = 90 |
| b = 124.07 | β = 90 |
| c = 134.11 | γ = 90 |
| Software Name | Purpose |
|---|---|
| CNS | refinement |
| MAR345 | data collection |
| XDS | data scaling |
| MOLREP | phasing |
Entry History
Deposition Data
- Released Date: 2006-05-09 Deposition Author(s): Gabdoulkhakov, A.G., Dontsova, M.V., Lashkov, A.A., Betzel, C., Ealick, S., Mikhailov, A.M.
Revision History (Full details and data files)
- Version 1.0: 2006-05-09
Type: Initial release - Version 1.1: 2008-04-30
Changes: Version format compliance - Version 1.2: 2011-07-13
Changes: Source and taxonomy, Version format compliance - Version 1.3: 2017-10-11
Changes: Refinement description - Version 1.4: 2017-10-18
Changes: Structure summary - Version 1.5: 2023-08-23
Changes: Data collection, Database references, Derived calculations, Refinement description
