1i7w

BETA-CATENIN/PHOSPHORYLATED E-CADHERIN COMPLEX

Method: X-RAY DIFFRACTION Dmax: 158.3 Å Quality: GOOD

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 134–671 Chain C; UniProt 134–671 Fragment:ARMADILLO DOMAIN EPITHELIAL-CADHERIN × 2 (P09803) ZN ZINC ION × 2 CL CHLORIDE ION × 8 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;293 K;polyethylene glycol monomethylether 5000, Tris-HCl, NaCl, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.00 Å R-free 0.245

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 19 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 C; PDBConstruct 1–538; UniProt 134–671

EPITHELIAL-CADHERIN

Mus musculus

UniProt P09803

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 734–884 Chain D; UniProt 734–884 Fragment:CYTOPLASMIC DOMAIN Non-standard monomer:Yes (specific site not provided by mmCIF) BETA-CATENIN × 2 (Q02248) ZN ZINC ION × 2 CL CHLORIDE ION × 8 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;293 K;polyethylene glycol monomethylether 5000, Tris-HCl, NaCl, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.00 Å R-free 0.245

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.

19 other PDB entries and 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CADH1_MOUSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–151; UniProt 734–884 Author chain D; PDBConstruct 1–151; UniProt 734–884

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 1i7w

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1i7w
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1i7w
Deposition date deposition_date2001-03-10
Structure title titleBETA-CATENIN/PHOSPHORYLATED E-CADHERIN COMPLEX
Keywords keywordsE-cadherin, cell adhesion, beta-catenin, protein-protein complex, extended interface, armadillo repeat, phosphoserine; CELL ADHESION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier42.82
Radius of gyration Rg (electron density) rg_electron43.37
Forward intensity I(0) i0227727000.00
Molecular weight molecular_weight121980.0 kDa
Excluded volume excluded_volume152620 ų
Envelope volume envelope_volume204770 ų
Hydration-shell volume shell_volume43135 ų
Envelope diameter envelope_diameter168.1
Shell Rg shell_rg42.92
Envelope Rg envelope_rg43.65
Shape Rg shape_rg43.40
Total Rg total_rg43.22
Total atoms total_atoms8522
Residues n_residues1114
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 dmax158.3
Rg (real space) rg_real43.35
Rg uncertainty (real space) rg_real_error2.01
I(0) (real space) i0_real2.2770e+08
I(0) uncertainty (real space) i0_real_error4.3580e+06
Rg (reciprocal space) rg_reciprocal42.82
I(0) (reciprocal space) i0_reciprocal227600000.0000
Solution quality estimate total_estimate0.7794
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary51.3
Skewness Skewness skewness0.659
Kurtosis Kurtosis kurtosis0.185
Angular range angular_range— – 0.1850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha13750000.0000
Real-space data points n_real_points38
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.598; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.682; Smooth: 0.652

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd1i7wa_
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_idd1i7wb_
Class classj — Peptides
Fold Fold foldj.71 — beta-Catenine bound non-globular protein regions
Superfamily Superfamily superfamilyj.71.1 — beta-Catenine bound non-globular protein regions
Family Family familyj.71.1.1 — beta-Catenine bound non-globular protein regions
Domain ID domain_idd1i7wc_
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_idd1i7wd_
Class classj — Peptides
Fold Fold foldj.71 — beta-Catenine bound non-globular protein regions
Superfamily Superfamily superfamilyj.71.1 — beta-Catenine bound non-globular protein regions
Family Family familyj.71.1.1 — beta-Catenine bound non-globular protein regions

CATH v4.4 (4 domains)

Domain ID domain_id1i7wA00
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_id1i7wB00
Class class4 — Few Secondary Structures
Architecture architecture10 — Irregular
Topology topology900 — TCF3-CBD (Catenin binding domain)
Homologous superfamily homologous superfamily10 — TCF3-CBD (Catenin binding domain)
Domain ID domain_id1i7wC00
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_id1i7wD00
Class class4 — Few Secondary Structures
Architecture architecture10 — Irregular
Topology topology900 — TCF3-CBD (Catenin binding domain)
Homologous superfamily homologous superfamily10 — TCF3-CBD (Catenin binding domain)

8. Citations (4)

9. Files and Curves (10)