4QWW
Crystal structure of the Fab410-BfAChE complex
- PDB DOI: https://doi.org/10.2210/pdb4QWW/pdb
- Classification: HYDROLASE/IMMUNE SYSTEM
- Organism(s): Bungarus fasciatus, Mus musculus
- Mutation(s): No
- Membrane Protein: Yes OPM
- Deposited: 2014-07-17 Released: 2014-11-26
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.70 Å
- R-Value Free: 0.239
- R-Value Work: 0.199
- R-Value Observed: 0.201
This is version 2.1 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 | 542 | Bungarus fasciatus | Mutation(s): 0 EC: 3.1.1.7 Membrane Entity: Yes |  | |
UniProt | |||||
Find proteins for Q92035 (Bungarus fasciatus) Explore Q92035 Go to UniProtKB: Q92035 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q92035 | ||||
Sequence AnnotationsExpand | |||||
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Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 2 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| Fab410 antibody light chain | 213 | Mus musculus | Mutation(s): 0 |  | |
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
Sequence AnnotationsExpand | |||||
| |||||
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 3 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| Fab410 antibody heavy chain | 234 | Mus musculus | Mutation(s): 0 |  | |
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
Sequence AnnotationsExpand | |||||
| |||||
Oligosaccharides
Entity ID: 4 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Length | 2D Diagram | Glycosylation | 3D Interactions |
| alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose | G, I | 6 |  | N-Glycosylation | |
Glycosylation Resources | |||||
GlyTouCan: G82348BZ GlyCosmos: G82348BZ GlyGen: G82348BZ | |||||
Entity ID: 5 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Length | 2D Diagram | Glycosylation | 3D Interactions |
| alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose | H, J | 5 |  | N-Glycosylation | |
Glycosylation Resources | |||||
GlyTouCan: G22768VO GlyCosmos: G22768VO GlyGen: G22768VO | |||||
Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| NAG Query on NAG | L [auth B] | 2-acetamido-2-deoxy-beta-D-glucopyranose C8 H15 N O6 OVRNDRQMDRJTHS-FMDGEEDCSA-N |  | ||
| EDO Query on EDO | K [auth A], M [auth B] | 1,2-ETHANEDIOL C2 H6 O2 LYCAIKOWRPUZTN-UHFFFAOYSA-N |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 2.70 Å
- R-Value Free: 0.239
- R-Value Work: 0.199
- R-Value Observed: 0.201
- Space Group: P 21 21 2
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 156.592 | α = 90 |
| b = 251.336 | β = 90 |
| c = 73.978 | γ = 90 |
| Software Name | Purpose |
|---|---|
| ADSC | data collection |
| AMoRE | phasing |
| BUSTER | refinement |
| MOSFLM | data reduction |
| SCALA | data scaling |
Entry History
Deposition Data
- Released Date: 2014-11-26 Deposition Author(s): Bourne, Y., Renault, L., Marchot, P.
Revision History (Full details and data files)
- Version 1.0: 2014-11-26
Type: Initial release - Version 1.1: 2014-12-03
Changes: Database references - Version 1.2: 2015-02-11
Changes: Database references - Version 1.3: 2017-06-28
Changes: Database references - Version 2.0: 2020-07-29
Type: Remediation
Reason: Carbohydrate remediation
Changes: Atomic model, Data collection, Database references, Derived calculations, Structure summary - Version 2.1: 2023-09-20
Changes: Data collection, Database references, Refinement description, Structure summary
