8vmg

Crystal structure of GSK-3 26-383 bound to Axin 383-435

Method: X-RAY DIFFRACTION Dmax: 115.6 Å Quality: GOOD

1. Protein Identity and Related Structures Protein Identity & Related Structures

Glycogen synthase kinase-3 beta

Mus musculus

UniProt Q9WV60

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 26–383 Not recorded Axin-1 × 1 (O15169) ADP ADENOSINE-5'-DIPHOSPHATE × 1 EDO 1,2-ETHANEDIOL × 20 NO3 NITRATE ION × 8 GOL GLYCEROL × 4 SO4 SULFATE ION × 7 MG MAGNESIUM ION × 1 CL CHLORIDE ION × 7 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;298 K;100 mM MES, pH 5.5, 1.9 M ammonium sulfate, 200 mM sodium chloride, cryoprotectant: 25% ethylene glycol Resolution 2.45 Å R-free 0.230
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 26–383 Not recorded Axin-1 × 1 (O15169) EDO 1,2-ETHANEDIOL × 19 SO4 SULFATE ION × 2 CL CHLORIDE ION × 8 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;298 K;100 mM MES, pH 5.5, 1.9 M ammonium sulfate, 200 mM sodium chloride, cryoprotectant: 25% ethylene glycol Resolution 2.45 Å R-free 0.230

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

5 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GSK3B_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–358; UniProt 26–383 Author chain B; PDBConstruct 1–358; UniProt 26–383

Axin-1

Homo sapiens

UniProt O15169

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 383–435 Not recorded Glycogen synthase kinase-3 beta × 1 (Q9WV60) ADP ADENOSINE-5'-DIPHOSPHATE × 1 EDO 1,2-ETHANEDIOL × 20 NO3 NITRATE ION × 8 GOL GLYCEROL × 4 SO4 SULFATE ION × 7 MG MAGNESIUM ION × 1 CL CHLORIDE ION × 7 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;298 K;100 mM MES, pH 5.5, 1.9 M ammonium sulfate, 200 mM sodium chloride, cryoprotectant: 25% ethylene glycol Resolution 2.45 Å R-free 0.230
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 383–435 Not recorded Glycogen synthase kinase-3 beta × 1 (Q9WV60) EDO 1,2-ETHANEDIOL × 19 SO4 SULFATE ION × 2 CL CHLORIDE ION × 8 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;298 K;100 mM MES, pH 5.5, 1.9 M ammonium sulfate, 200 mM sodium chloride, cryoprotectant: 25% ethylene glycol Resolution 2.45 Å R-free 0.230

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

15 other PDB entries and 22 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name AXIN1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 8–60; UniProt 383–435 Author chain D; PDBConstruct 8–60; UniProt 383–435

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 8vmg

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8vmg
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8vmg
Deposition date deposition_date2024-01-13
Structure title titleCrystal structure of GSK-3 26-383 bound to Axin 383-435
Keywords keywordsGSK-3, kinase, TRANSFERASE-SIGNALING PROTEIN complex; TRANSFERASE/SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier32.37
Radius of gyration Rg (electron density) rg_electron31.73
Forward intensity I(0) i0137075000.00
Molecular weight molecular_weight91795.0 kDa
Excluded volume excluded_volume114340 ų
Envelope volume envelope_volume147730 ų
Hydration-shell volume shell_volume39551 ų
Envelope diameter envelope_diameter125.5
Shell Rg shell_rg37.68
Envelope Rg envelope_rg32.32
Shape Rg shape_rg31.71
Total Rg total_rg32.27
Total atoms total_atoms6682
Residues n_residues778
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax115.6
Rg (real space) rg_real32.49
Rg uncertainty (real space) rg_real_error1.08
I(0) (real space) i0_real1.3710e+08
I(0) uncertainty (real space) i0_real_error2.3580e+06
Rg (reciprocal space) rg_reciprocal32.44
I(0) (reciprocal space) i0_reciprocal137100000.0000
Solution quality estimate total_estimate0.8484
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary35.4
Skewness Skewness skewness0.468
Kurtosis Kurtosis kurtosis-0.151
Angular range angular_range— – 0.2450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha35790000.0000
Real-space data points n_real_points50
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.731; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.922; Smooth: 0.909

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (11)

8. Citations (1)

9. Files and Curves (10)