Download MendeleyMethylphosphonate Adducts of Acetylcholinesterase Investigated by Time Correlated Single Photon Counting and X-Ray Crystallography
Akfur, C., Artursson, E., Ekstrom, F.To be published.
2Y2U
Nonaged form of Mouse Acetylcholinesterase inhibited by VX-Update
- PDB DOI: https://doi.org/10.2210/pdb2Y2U/pdb
- Entry: 2Y2U supersedes: 2JGH
- Classification: HYDROLASE
- Organism(s): Mus musculus
- Expression System: Homo sapiens
- Mutation(s): No
- Deposited: 2010-12-16 Released: 2011-11-30
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.60 Å
- R-Value Free: 0.237
- R-Value Work: 0.188
- R-Value Observed: 0.189
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 |
| ACETYLCHOLINESTERASE | 548 | Mus musculus | Mutation(s): 0 EC: 3.1.1.7 |  | |
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for P21836 (Mus musculus) Explore P21836 Go to UniProtKB: P21836 | |||||
IMPC: MGI:87876 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | P21836 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 3 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| P33 Query on P33 | K [auth B] | 3,6,9,12,15,18-HEXAOXAICOSANE-1,20-DIOL C14 H30 O8 XPJRQAIZZQMSCM-UHFFFAOYSA-N |  | ||
| NAG Query on NAG | C [auth A], D [auth A], H [auth B] | 2-acetamido-2-deoxy-beta-D-glucopyranose C8 H15 N O6 OVRNDRQMDRJTHS-FMDGEEDCSA-N |  | ||
| PEG Query on PEG | E [auth A], F [auth A], G [auth A], I [auth B], J [auth B] | DI(HYDROXYETHYL)ETHER C4 H10 O3 MTHSVFCYNBDYFN-UHFFFAOYSA-N |  | ||
| Modified Residues 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Type | Formula | 2D Diagram | Parent |
| SVX Query on SVX | A, B | L-PEPTIDE LINKING | C6 H14 N O5 P |  | SER |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 2.60 Å
- R-Value Free: 0.237
- R-Value Work: 0.188
- R-Value Observed: 0.189
- Space Group: P 21 21 21
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 78.914 | α = 90 |
| b = 110.368 | β = 90 |
| c = 227.178 | γ = 90 |
| Software Name | Purpose |
|---|---|
| PHENIX | refinement |
| XDS | data reduction |
| SCALA | data scaling |
| REFMAC | phasing |
Entry History
Deposition Data
- Released Date: 2011-11-30 Deposition Author(s): Akfur, C., Artursson, E., Ekstrom, F.
- This entry supersedes: 2JGH
Revision History (Full details and data files)
- Version 1.0: 2011-11-30
Type: Initial release - Version 1.1: 2018-01-17
Changes: Data collection - Version 1.2: 2020-07-29
Type: Remediation
Reason: Carbohydrate remediation
Changes: Data collection, Derived calculations, Other, Structure summary - Version 1.3: 2023-12-20
Changes: Data collection, Database references, Refinement description, Structure summary
