1KU6
Fasciculin 2-Mouse Acetylcholinesterase Complex
- PDB DOI: https://doi.org/10.2210/pdb1KU6/pdb
- Classification: HYDROLASE/TOXIN
- Organism(s): Mus musculus, Dendroaspis angusticeps
- Expression System: Homo sapiens
- Mutation(s): No
- Deposited: 2002-01-21 Released: 2003-12-23
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.50 Å
- R-Value Free: 0.273
- R-Value Work: 0.226
This is version 1.3 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 | 549 | Mus musculus | Mutation(s): 0 |  | |
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 | |||||
| |||||
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 2 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| FASCICULIN 2 | 61 | Dendroaspis angusticeps | Mutation(s): 0 |  | |
UniProt | |||||
Find proteins for P0C1Z0 (Dendroaspis angusticeps) Explore P0C1Z0 Go to UniProtKB: P0C1Z0 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | P0C1Z0 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| NAG Query on NAG | C [auth A] | 2-acetamido-2-deoxy-beta-D-glucopyranose C8 H15 N O6 OVRNDRQMDRJTHS-FMDGEEDCSA-N |  | ||
| EDO Query on EDO | D [auth A] | 1,2-ETHANEDIOL C2 H6 O2 LYCAIKOWRPUZTN-UHFFFAOYSA-N |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 2.50 Å
- R-Value Free: 0.273
- R-Value Work: 0.226
- Space Group: P 65 2 2
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 73.8 | α = 90 |
| b = 73.8 | β = 90 |
| c = 548.62 | γ = 120 |
| Software Name | Purpose |
|---|---|
| DENZO | data reduction |
| SCALA | data scaling |
| CNS | refinement |
| CCP4 | data scaling |
| CNS | phasing |
Entry History
Deposition Data
- Released Date: 2003-12-23 Deposition Author(s): Bourne, Y., Burmeister, W., Taylor, P., Marchot, P.
Revision History (Full details and data files)
- Version 1.0: 2003-12-23
Type: Initial release - Version 1.1: 2008-04-27
Changes: Version format compliance - Version 1.2: 2011-07-13
Changes: Non-polymer description, Version format compliance - Version 1.3: 2020-07-29
Type: Remediation
Reason: Carbohydrate remediation
Changes: Advisory, Data collection, Derived calculations, Structure summary
