› 4nu1

X-ray diffraction
2.5Å resolution

Crystal structure of a transition state mimic of the GSK-3/Axin complex bound to phosphorylated N-terminal auto-inhibitory pS9 peptide

Released:
DOI: 10.2210/pdb4nu1/pdb
PDB 4nu1 coloured by chain and viewed from the front.
PDB 4nu1 coloured by chain and viewed from the side.
PDB 4nu1 coloured by chain and viewed from the top.
Source organisms:
Primary publication:
Structural basis of GSK-3 inhibition by N-terminal phosphorylation and by the Wnt receptor LRP6.
Stamos JL, Chu ML, Enos MD, Shah N, Weis WI
Elife 3 e01998 (2014)
PMID: 24642411

Function and Biology Details

Reaction catalysed: 
ATP + [tau protein] = ADP + [tau protein] phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Glycogen synthase kinase-3 beta Chain: A
Molecule details ›
Chain: A
Length: 389 amino acids
Theoretical weight: 44.26 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9WV60 (Residues: 1-383; Coverage: 91%)
Gene name: Gsk3b
Sequence domains: Protein kinase domain
Structure domains:
Axin-1 Chain: B
Molecule details ›
Chain: B
Length: 24 amino acids
Theoretical weight: 2.74 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O15169 (Residues: 383-402; Coverage: 2%)
Gene names: AXIN, AXIN1

Ligands and Environments

5 bound ligands:
Ligand GOL 2 x GOL
Ligand MG 2 x MG
Ligand ADP 1 x ADP
Ligand AF3 1 x AF3
Ligand NO3 1 x NO3
1 modified residue:
Ligand SEP 1 x SEP

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-B
Spacegroup: P6122
Unit cell:
a: 80.997Å b: 80.997Å c: 280.53Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.194 0.191 0.245
Expression system: Escherichia coli

Quick links

Citations

24 review citations

Cross-Talk between Wnt Signaling and Src Tyrosine Kinase.
Min et al. (2022)
23 more

2 mentions without citation

Structural basis of GSK-3 inhibition by N-terminal phosphorylation and by the Wnt receptor LRP6.
Stamos et al. (2014)
1 more