3HKL
Crystal Structure of the Frizzled-like Cysteine-rich Domain of MuSK
- PDB DOI: https://doi.org/10.2210/pdb3HKL/pdb
- Classification: Transferase,Signaling protein
- Organism(s): Rattus norvegicus
- Expression System: Spodoptera frugiperda
- Mutation(s): No 
- Deposited: 2009-05-24 Released: 2009-08-25 
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.10 Å
- R-Value Free: 0.264 
- R-Value Work: 0.226 
- R-Value Observed: 0.228 
wwPDB Validation   3D Report Full Report
This is version 2.0 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 |
Muscle, skeletal receptor tyrosine protein kinase | 197 | Rattus norvegicus | Mutation(s): 0  Gene Names: Musk EC: 2.7.10.1 | ||
UniProt | |||||
Find proteins for Q62838 (Rattus norvegicus) Explore Q62838  Go to UniProtKB:  Q62838 | |||||
Entity Groups   | |||||
Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
UniProt Group | Q62838 | ||||
Sequence AnnotationsExpand | |||||
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Oligosaccharides
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 2.10 Å
- R-Value Free: 0.264 
- R-Value Work: 0.226 
- R-Value Observed: 0.228 
- Space Group: P 1 21 1
Unit Cell:
Length ( Å ) | Angle ( ˚ ) |
---|---|
a = 65.592 | α = 90 |
b = 44.422 | β = 108.27 |
c = 69.53 | γ = 90 |
Software Name | Purpose |
---|---|
REFMAC | refinement |
HKL-2000 | data collection |
HKL-2000 | data reduction |
HKL-2000 | data scaling |
Entry History 
Deposition Data
- Released Date: 2009-08-25  Deposition Author(s): Stiegler, A.L., Hubbard, S.R.
Revision History (Full details and data files)
- Version 1.0: 2009-08-25
Type: Initial release - Version 1.1: 2011-07-13
Changes: Non-polymer description, Version format compliance - Version 2.0: 2020-07-29
Type: Remediation
Reason: Carbohydrate remediation
Changes: Atomic model, Data collection, Database references, Derived calculations, Structure summary