1dow

CRYSTAL STRUCTURE OF A CHIMERA OF BETA-CATENIN AND ALPHA-CATENIN

Method: X-RAY DIFFRACTION Dmax: 98.6 Å Quality: REASONABLE

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

ALPHA-CATENIN

Mus musculus

UniProt P26231

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 57–261 Fragment:DIMERIZATION AND BETA-CATENIN BINDING REGION Non-standard monomer:Yes (specific site not provided by mmCIF) BETA-CATENIN × 1 (Q02248) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;295 K;PEG 2000 monomethylether, HEPES, urea, ethanol, Dithiothreitol, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 295.0K Resolution 1.80 Å R-free 0.233

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.

9 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CTN1_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–205; UniProt 57–261

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 B; UniProt 118–149 Fragment:ALPHA-CATENIN BINDING REGION Non-standard monomer:Yes (specific site not provided by mmCIF) ALPHA-CATENIN × 1 (P26231) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;295 K;PEG 2000 monomethylether, HEPES, urea, ethanol, Dithiothreitol, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 295.0K Resolution 1.80 Å R-free 0.233

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 2
Chains and sequence ranges Author chain B; PDBConstruct 1–32; UniProt 118–149

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 1dow

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1dow
Deposition date deposition_date1999-12-21
Structure title titleCRYSTAL STRUCTURE OF A CHIMERA OF BETA-CATENIN AND ALPHA-CATENIN
Keywords keywordsfour-helix bundle, 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_guinier25.92
Radius of gyration Rg (electron density) rg_electron25.97
Forward intensity I(0) i012634500.00
Molecular weight molecular_weight26300.0 kDa
Excluded volume excluded_volume32691 ų
Envelope volume envelope_volume40154 ų
Hydration-shell volume shell_volume15537 ų
Envelope diameter envelope_diameter102.7
Shell Rg shell_rg28.24
Envelope Rg envelope_rg26.39
Shape Rg shape_rg26.04
Total Rg total_rg26.06
Total atoms total_atoms1824
Residues n_residues231
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 dmax98.6
Rg (real space) rg_real26.46
Rg uncertainty (real space) rg_real_error1.22
I(0) (real space) i0_real1.2630e+07
I(0) uncertainty (real space) i0_real_error2.3740e+05
Rg (reciprocal space) rg_reciprocal26.30
I(0) (reciprocal space) i0_reciprocal12630000.0000
Solution quality estimate total_estimate0.6947
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary17.8
Skewness Skewness skewness0.710
Kurtosis Kurtosis kurtosis-0.113
Angular range angular_range— – 0.3050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2237000.0000
Real-space data points n_real_points62
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.323; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.085; Smooth: 0.974

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1dowa_
Class classa — All alpha proteins
Fold Fold folda.24 — Four-helical up-and-down bundle
Superfamily Superfamily superfamilya.24.9 — alpha-catenin/vinculin-like
Family Family familya.24.9.1 — alpha-catenin/vinculin

CATH v4.4 (1 domains)

Domain ID domain_id1dowA00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology120 — Four Helix Bundle (Hemerythrin (Met), subunit A)
Homologous superfamily homologous superfamily230 — Alpha-catenin/vinculin-like

8. Citations (1)

9. Files and Curves (10)