1g3j

CRYSTAL STRUCTURE OF THE XTCF3-CBD/BETA-CATENIN ARMADILLO REPEAT COMPLEX

Method: X-RAY DIFFRACTION Dmax: 140.4 Å Quality: GOOD

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

BETA-CATENIN ARMADILLO REPEAT REGION

Homo sapiens

UniProt P35222

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 133–664 Not recorded TCF3-CBD (CATENIN BINDING DOMAIN) × 1 (P70062) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.2;298 K;2.5% PEG-8000, 44mM Phosphate-Citrate, 2mM DTT, pH 4.2, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K Resolution 2.10 Å R-free 0.255
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 133–664 Not recorded TCF3-CBD (CATENIN BINDING DOMAIN) × 1 (P70062) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.2;298 K;2.5% PEG-8000, 44mM Phosphate-Citrate, 2mM DTT, pH 4.2, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K Resolution 2.10 Å R-free 0.255

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.

46 other PDB entries and 63 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CTNB1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–532; UniProt 133–664 Author chain C; PDBConstruct 1–532; UniProt 133–664

TCF3-CBD (CATENIN BINDING DOMAIN)

Xenopus laevis

UniProt P70062

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 1–61 Not recorded BETA-CATENIN ARMADILLO REPEAT REGION × 1 (P35222) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.2;298 K;2.5% PEG-8000, 44mM Phosphate-Citrate, 2mM DTT, pH 4.2, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K Resolution 2.10 Å R-free 0.255
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 1–61 Not recorded BETA-CATENIN ARMADILLO REPEAT REGION × 1 (P35222) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.2;298 K;2.5% PEG-8000, 44mM Phosphate-Citrate, 2mM DTT, pH 4.2, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K Resolution 2.10 Å R-free 0.255

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name P70062_XENLA
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–61; UniProt 1–61 Author chain D; PDBConstruct 1–61; UniProt 1–61

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 1g3j

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1g3j
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1g3j
Deposition date deposition_date2000-10-24
Structure title titleCRYSTAL STRUCTURE OF THE XTCF3-CBD/BETA-CATENIN ARMADILLO REPEAT COMPLEX
Keywords keywordsBeta-catenin, Tcf-3, Protein-Protein Complex, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier39.65
Radius of gyration Rg (electron density) rg_electron40.37
Forward intensity I(0) i0176614000.00
Molecular weight molecular_weight107360.0 kDa
Excluded volume excluded_volume134600 ų
Envelope volume envelope_volume176440 ų
Hydration-shell volume shell_volume40434 ų
Envelope diameter envelope_diameter148.5
Shell Rg shell_rg40.79
Envelope Rg envelope_rg40.59
Shape Rg shape_rg40.38
Total Rg total_rg40.34
Total atoms total_atoms7531
Residues n_residues1036
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 dmax140.4
Rg (real space) rg_real40.33
Rg uncertainty (real space) rg_real_error1.71
I(0) (real space) i0_real1.7660e+08
I(0) uncertainty (real space) i0_real_error3.1760e+06
Rg (reciprocal space) rg_reciprocal39.91
I(0) (reciprocal space) i0_reciprocal176500000.0000
Solution quality estimate total_estimate0.7876
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary45.6
Skewness Skewness skewness0.667
Kurtosis Kurtosis kurtosis0.039
Angular range angular_range— – 0.2000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha13930000.0000
Real-space data points n_real_points41
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.695; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.680; Smooth: 0.471

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 7 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd1g3ja_
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_idd1g3jb_
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_idd1g3jc_
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_idd1g3jd_
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 (3 domains)

Domain ID domain_id1g3jA00
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_id1g3jB00
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_id1g3jC00
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology10 — Leucine-rich Repeat Variant
Homologous superfamily homologous superfamily10 — Leucine-rich Repeat Variant

8. Citations (1)

9. Files and Curves (10)