Download MendeleyStereo-selectively Induced Cofactor Switching Provides Insight into Cofactor Site Plasticity as a Possible Mechanism of Antifolate Resistance
Keshipeddy, S., Reeve, S.M., Anderson, A.C., Wright, D.L.To be published.
4XE6
Staphylococcus aureus Dihydrofolate Reductase complexed with NADPH and 6-ETHYL-5-[(3R)-3-[3-METHOXY-5-(PYRIDIN-4-YL)PHENYL]BUT-1-YN-1-YL]PYRIMIDINE-2,4-DIAMINE (UCP1061)
- PDB DOI: https://doi.org/10.2210/pdb4XE6/pdb
- Classification: OXIDOREDUCTASE/OXIDOREDUCTASE Inhibitor
- Organism(s): Staphylococcus aureus
- Expression System: Escherichia coli BL21
- Mutation(s): No
- Deposited: 2014-12-23 Released: 2016-01-20
- Funding Organization(s): National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.69 ?
- R-Value Free: 0.232
- R-Value Work: 0.158
- R-Value Observed: 0.165
Starting Model: experimental
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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 |
| Dihydrofolate reductase | A [auth X] | 160 | Staphylococcus aureus | Mutation(s): 0 Gene Names: folA EC: 1.5.1.3 |  |
UniProt | |||||
Find proteins for P0A017 (Staphylococcus aureus) Explore P0A017 Go to UniProtKB: P0A017 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | P0A017 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 3 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| NDP Query on NDP | D [auth X] | NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE C21 H30 N7 O17 P3 ACFIXJIJDZMPPO-NNYOXOHSSA-N |  | ||
| 06U Query on 06U | B [auth X] | 6-ethyl-5-{(3R)-3-[3-methoxy-5-(pyridin-4-yl)phenyl]but-1-yn-1-yl}pyrimidine-2,4-diamine C22 H23 N5 O KEPLBUUTAQCZOE-AWEZNQCLSA-N |  | ||
| ACT Query on ACT | C [auth X] | ACETATE ION C2 H3 O2 QTBSBXVTEAMEQO-UHFFFAOYSA-M |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 2.69 ?
- R-Value Free: 0.232
- R-Value Work: 0.158
- R-Value Observed: 0.165
- Space Group: P 61 2 2
Unit Cell:
| Length ( ? ) | Angle ( ? ) |
|---|---|
| a = 78.902 | ¦Á = 90 |
| b = 78.902 | ¦Â = 90 |
| c = 108.118 | ¦Ă = 120 |
| Software Name | Purpose |
|---|---|
| PHENIX | refinement |
| HKL-2000 | data reduction |
| HKL-2000 | data scaling |
| PHENIX | phasing |
Entry History & Funding Information
Deposition Data
- Released Date: 2016-01-20 Deposition Author(s): Reeve, S.M., Anderson, A.C.
| Funding Organization | Location | Grant Number |
|---|---|---|
| National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID) | United States | AI111957 |
Revision History (Full details and data files)
- Version 1.0: 2016-01-20
Type: Initial release - Version 1.1: 2017-09-20
Changes: Author supporting evidence, Derived calculations - Version 1.2: 2019-12-11
Changes: Author supporting evidence - Version 1.3: 2023-09-27
Changes: Data collection, Database references, Refinement description
