Download MendeleyStructural Studies of Early Events in Catalysis by Thymidylate Synthase
Arendall III, W.B., Hyatt, D.C., Roberts, S.A., Weichsel, A., Dahlgren, A.L., Maley, F., Montfort, W.R.To be published.
3BHR
E. coli TS complexed with 5-NO2dUMP and tetrahydrofolate at 1.9 A resolution (space group 152)
- PDB DOI: https://doi.org/10.2210/pdb3BHR/pdb
- Classification: TRANSFERASE
- Organism(s): Escherichia coli
- Expression System: Escherichia coli
- Mutation(s): No
- Deposited: 2007-11-28 Released: 2008-12-02
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.90 Å
- R-Value Free: 0.201
- R-Value Work: 0.167
- R-Value Observed: 0.168
This is version 1.4 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 synthase | 264 | Escherichia coli | Mutation(s): 0 Gene Names: thyA EC: 2.1.1.45 |  | |
UniProt | |||||
Find proteins for P0A884 (Escherichia coli (strain K12)) Explore P0A884 Go to UniProtKB: P0A884 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | P0A884 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 3 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| THG Query on THG | C [auth A] | (6S)-5,6,7,8-TETRAHYDROFOLATE C19 H23 N7 O6 MSTNYGQPCMXVAQ-RYUDHWBXSA-N |  | ||
| NDU Query on NDU | E [auth A] | 2'-DEOXY-5-NITROURIDINE 5'-MONOPHOSPHATE C9 H14 N3 O10 P ZYBJIJYGXJSDTC-XZBKPIIZSA-N |  | ||
| PO4 Query on PO4 | B [auth A], D [auth A] | PHOSPHATE ION O4 P NBIIXXVUZAFLBC-UHFFFAOYSA-K |  | ||
| Modified Residues 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Type | Formula | 2D Diagram | Parent |
| CXM Query on CXM | A | L-PEPTIDE LINKING | C6 H11 N O4 S |  | MET |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.90 Å
- R-Value Free: 0.201
- R-Value Work: 0.167
- R-Value Observed: 0.168
- Space Group: P 31 2 1
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 71.95 | α = 90 |
| b = 71.95 | β = 90 |
| c = 115.47 | γ = 120 |
| Software Name | Purpose |
|---|---|
| REFMAC | refinement |
| MADNESS | data collection |
| PROCOR | data reduction |
| PROCOR | data scaling |
Entry History
Deposition Data
- Released Date: 2008-12-02 Deposition Author(s): Roberts, S.A., Montfort, W.R.
Revision History (Full details and data files)
- Version 1.0: 2008-12-02
Type: Initial release - Version 1.1: 2011-07-13
Changes: Non-polymer description, Version format compliance - Version 1.2: 2017-10-25
Changes: Refinement description - Version 1.3: 2018-04-18
Changes: Data collection - Version 1.4: 2024-10-30
Changes: Data collection, Database references, Derived calculations, Structure summary
