4ARA
Mus musculus Acetylcholinesterase in complex with (R)-C5685 at 2.5 A resolution.
- PDB DOI: https://doi.org/10.2210/pdb4ARA/pdb
- Classification: HYDROLASE
- Organism(s): Mus musculus
- Expression System: Homo sapiens
- Mutation(s): No 
- Deposited: 2012-04-23 Released: 2012-11-28 
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.50 Å
- R-Value Free: 0.222 
- R-Value Work: 0.183 
- R-Value Observed: 0.183 
This is version 2.3 of the entry. See complete history. 
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 | |||||
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Small Molecules
Ligands 6 Unique | |||||
---|---|---|---|---|---|
ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
C56 Query on C56 | C [auth A], N [auth B] | 4-(DIMETHYLAMINO)-N-{[(2R)-1-ETHYLPYRROLIDIN-2-YL]METHYL}-2-METHOXY-5-NITROBENZAMIDE C17 H26 N4 O4 AFNPLUMDSLEAPD-GFCCVEGCSA-N | |||
1PE Query on 1PE | P [auth B] | PENTAETHYLENE GLYCOL C10 H22 O6 JLFNLZLINWHATN-UHFFFAOYSA-N | |||
NAG Query on NAG | I [auth A], M [auth A], V [auth B] | 2-acetamido-2-deoxy-beta-D-glucopyranose C8 H15 N O6 OVRNDRQMDRJTHS-FMDGEEDCSA-N | |||
PEG Query on PEG | D [auth A] F [auth A] G [auth A] O [auth B] Q [auth B] | DI(HYDROXYETHYL)ETHER C4 H10 O3 MTHSVFCYNBDYFN-UHFFFAOYSA-N | |||
EDO Query on EDO | E [auth A] H [auth A] J [auth A] K [auth A] L [auth A] | 1,2-ETHANEDIOL C2 H6 O2 LYCAIKOWRPUZTN-UHFFFAOYSA-N | |||
CL Query on CL | Y [auth B] | CHLORIDE ION Cl VEXZGXHMUGYJMC-UHFFFAOYSA-M |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 2.50 Å
- R-Value Free: 0.222 
- R-Value Work: 0.183 
- R-Value Observed: 0.183 
- Space Group: P 21 21 21
Unit Cell:
Length ( Å ) | Angle ( ˚ ) |
---|---|
a = 78.764 | α = 90 |
b = 112.012 | β = 90 |
c = 227.34 | γ = 90 |
Software Name | Purpose |
---|---|
PHENIX | refinement |
XDS | data reduction |
SCALA | data scaling |
REFMAC | phasing |
Entry History 
Deposition Data
- Released Date: 2012-11-28  Deposition Author(s): Berg, L., Niemiec, M.S., Qian, W., Andersson, C.D., WittungStafshede, P., Ekstrom, F., Linusson, A.
Revision History (Full details and data files)
- Version 1.0: 2012-11-28
Type: Initial release - Version 1.1: 2013-01-16
Changes: Database references - Version 2.0: 2018-01-17
Changes: Atomic model, Data collection - Version 2.1: 2018-02-28
Changes: Source and taxonomy - Version 2.2: 2020-07-29
Type: Remediation
Reason: Carbohydrate remediation
Changes: Data collection, Derived calculations, Other, Structure summary - Version 2.3: 2023-12-20
Changes: Data collection, Database references, Refinement description, Structure summary