1qz7

Beta-catenin binding domain of Axin in complex with beta-catenin

Method: X-RAY DIFFRACTION Dmax: 114.4 Å Quality: REASONABLE

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

Beta-catenin

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 133–665 Fragment:Armadillo repeat region Axin × 1 (Q9YGY0) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.6;298 K;PEG 6000, sodium citrate, isopropanol, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.20 Å R-free 0.256

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 64 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 1–533; UniProt 133–665

Axin

Xenopus laevis

UniProt Q9YGY0

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 435–504 Fragment:Beta-catenin binding domain Beta-catenin × 1 (P35222) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.6;298 K;PEG 6000, sodium citrate, isopropanol, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.20 Å R-free 0.256

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 AXN_XENLA
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–70; UniProt 435–504

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 1qz7

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1qz7
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1qz7
Deposition date deposition_date2003-09-15
Structure title titleBeta-catenin binding domain of Axin in complex with beta-catenin
Keywords keywordsBeta-catenin, Axin, protein-protein complex, 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_guinier33.67
Radius of gyration Rg (electron density) rg_electron33.77
Forward intensity I(0) i055592900.00
Molecular weight molecular_weight58818.0 kDa
Excluded volume excluded_volume73678 ų
Envelope volume envelope_volume95074 ų
Hydration-shell volume shell_volume26218 ų
Envelope diameter envelope_diameter120.1
Shell Rg shell_rg36.34
Envelope Rg envelope_rg33.60
Shape Rg shape_rg33.80
Total Rg total_rg33.89
Total atoms total_atoms4117
Residues n_residues541
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 dmax114.4
Rg (real space) rg_real34.12
Rg uncertainty (real space) rg_real_error1.45
I(0) (real space) i0_real5.5590e+07
I(0) uncertainty (real space) i0_real_error9.7660e+05
Rg (reciprocal space) rg_reciprocal33.84
I(0) (reciprocal space) i0_reciprocal55580000.0000
Solution quality estimate total_estimate0.7349
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.4
Skewness Skewness skewness0.580
Kurtosis Kurtosis kurtosis-0.457
Angular range angular_range— – 0.2350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8277000.0000
Real-space data points n_real_points48
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.592; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.307; Smooth: 0.470

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_idd1qz7a_
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 (1 domains)

Domain ID domain_id1qz7A00
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)