1jpp

The Structure of a beta-Catenin Binding Repeat from Adenomatous Polyposis Coli (APC) in Complex with beta-Catenin

Method: X-RAY DIFFRACTION Dmax: 315.2 Å Quality: REASONABLE

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

BETA-CATENIN

Mus musculus

UniProt Q02248

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 134–671 Not recorded ADENOMATOUS POLYPOSIS COLI PROTEIN × 1 (P25054) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.2;293 K;PEG 8000, sodium potassium phosphate, sodium chloride, DTT, pH 6.2, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 3.10 Å R-free 0.274
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 134–671 Not recorded ADENOMATOUS POLYPOSIS COLI PROTEIN × 1 (P25054) GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.2;293 K;PEG 8000, sodium potassium phosphate, sodium chloride, DTT, pH 6.2, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 3.10 Å R-free 0.274

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 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CTNB1_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–538; UniProt 134–671 Author chain B; PDBConstruct 1–538; UniProt 134–671

ADENOMATOUS POLYPOSIS COLI PROTEIN

OrganismNot specified

UniProt P25054

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 1021–1035 Not recorded BETA-CATENIN × 1 (Q02248) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.2;293 K;PEG 8000, sodium potassium phosphate, sodium chloride, DTT, pH 6.2, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 3.10 Å R-free 0.274
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 1021–1035 Not recorded BETA-CATENIN × 1 (Q02248) GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.2;293 K;PEG 8000, sodium potassium phosphate, sodium chloride, DTT, pH 6.2, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 3.10 Å R-free 0.274

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.

27 other PDB entries and 46 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name APC_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–15; UniProt 1021–1035 Author chain D; PDBConstruct 1–15; UniProt 1021–1035

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 1jpp

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1jpp
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1jpp
Deposition date deposition_date2001-08-02
Structure title titleThe Structure of a beta-Catenin Binding Repeat from Adenomatous Polyposis Coli (APC) in Complex with beta-Catenin
Keywords keywordsDisease mutation, Anti-oncogene, CELL ADHESION; CELL ADHESION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier93.00
Radius of gyration Rg (electron density) rg_electron93.85
Forward intensity I(0) i0167332000.00
Molecular weight molecular_weight111070.0 kDa
Excluded volume excluded_volume139740 ų
Envelope volume envelope_volume363670 ų
Hydration-shell volume shell_volume32696 ų
Envelope diameter envelope_diameter229.5
Shell Rg shell_rg104.10
Envelope Rg envelope_rg80.95
Shape Rg shape_rg93.89
Total Rg total_rg93.80
Total atoms total_atoms7778
Residues n_residues1026
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 dmax315.2
Rg (real space) rg_real93.87
Rg uncertainty (real space) rg_real_error5.90
I(0) (real space) i0_real1.6730e+08
I(0) uncertainty (real space) i0_real_error4.6150e+06
Rg (reciprocal space) rg_reciprocal86.38
I(0) (reciprocal space) i0_reciprocal163800000.0000
Solution quality estimate total_estimate0.5429
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks4
Primary peak position r_peak_primary185.4
Skewness Skewness skewness-0.069
Kurtosis Kurtosis kurtosis-1.756
Angular range angular_range— – 0.0850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6255000.0000
Real-space data points n_real_points18
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.000; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.053; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1jppa_
Class classa — All alpha proteins
Fold Fold folda.118 — alpha-alpha superhelix
Superfamily Superfamily superfamilya.118.1 — ARM repeat
Family Family familya.118.1.1 — Armadillo repeat
Domain ID domain_idd1jppb_
Class classa — All alpha proteins
Fold Fold folda.118 — alpha-alpha superhelix
Superfamily Superfamily superfamilya.118.1 — ARM repeat
Family Family familya.118.1.1 — Armadillo repeat

CATH v4.4 (2 domains)

Domain ID domain_id1jppA00
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology10 — Leucine-rich Repeat Variant
Homologous superfamily homologous superfamily10 — Leucine-rich Repeat Variant
Domain ID domain_id1jppB00
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology10 — Leucine-rich Repeat Variant
Homologous superfamily homologous superfamily10 — Leucine-rich Repeat Variant

8. Citations (4)

9. Files and Curves (10)