Download MendeleyMouse thymidylate synthase does not show the inactive conformation, observed for the human enzyme
Dowiercial, A., Jarmula, A., Wilk, P., Rypniewski, W., Kowalska, M., Fraczyk, T., Ciesla, J., Rode, W.(2016) Struct Chem
5FCT
Mouse thymidylate synthase in ternary complex with FdUMP and methylenetetrahydrofolate.
- PDB DOI: https://doi.org/10.2210/pdb5FCT/pdb
- Classification: TRANSFERASE
- Organism(s): Mus musculus
- Expression System: Escherichia coli
- Mutation(s): No
- Deposited: 2015-12-15 Released: 2016-10-26
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.55 Å
- R-Value Free: 0.166
- R-Value Work: 0.117
- R-Value Observed: 0.120
Starting Model: experimental
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This is version 1.4 of the entry. See complete history.
Literature
Macromolecules
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(by identity cutoff) | 3D Structure
Entity ID: 1 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| Thymidylate synthase | 307 | Mus musculus | Mutation(s): 0 Gene Names: Tyms, mCG_11630 EC: 2.1.1.45 |  | |
UniProt | |||||
Find proteins for P07607 (Mus musculus) Explore P07607 Go to UniProtKB: P07607 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | P07607 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| C2F Query on C2F | D [auth A], F [auth B] | 5-METHYL-5,6,7,8-TETRAHYDROFOLIC ACID C20 H25 N7 O6 ZNOVTXRBGFNYRX-STQMWFEESA-N |  | ||
| UFP Query on UFP | C [auth A], E [auth B] | 5-FLUORO-2'-DEOXYURIDINE-5'-MONOPHOSPHATE C9 H12 F N2 O8 P HFEKDTCAMMOLQP-RRKCRQDMSA-N |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.55 Å
- R-Value Free: 0.166
- R-Value Work: 0.117
- R-Value Observed: 0.120
- Space Group: P 1 21 1
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 54.224 | α = 90 |
| b = 83.302 | β = 105.43 |
| c = 68.85 | γ = 90 |
| Software Name | Purpose |
|---|---|
| REFMAC | refinement |
| CrysalisPro | data reduction |
| CrysalisPro | data scaling |
| CrysalisPro | phasing |
Entry History
Deposition Data
- Released Date: 2016-10-26 Deposition Author(s): Dowiercial, A., Wilk, P., Jarmula, A., Rode, W.
Revision History (Full details and data files)
- Version 1.0: 2016-10-26
Type: Initial release - Version 1.1: 2017-09-13
Changes: Data collection - Version 1.2: 2018-04-04
Changes: Data collection - Version 1.3: 2024-01-10
Changes: Data collection, Database references, Refinement description - Version 1.4: 2024-11-06
Changes: Structure summary
