9i8w

Beta-catenin armadillo with cyclic peptide and Compound 3

Method: X-RAY DIFFRACTION Dmax: 118.8 Å Quality: REASONABLE

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

Catenin beta-1

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 134–671 Not recorded Cyclic peptide × 1 HHT 2-(4-bromanyl-2-methoxy-phenyl)ethanoic acid × 1 SO4 SULFATE ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;0.1 M ADA pH 6.5, 100 mM ammonium sulfate, 30 % w/v PEG MME 5000 Resolution 2.20 Å R-free 0.244

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 1–538; UniProt 134–671

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 9i8w

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9i8w
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9i8w
Deposition date deposition_date2025-02-06
Structure title titleBeta-catenin armadillo with cyclic peptide and Compound 3
Keywords keywordsBeta-catenin armadillo, cyclic peptide, ONCOPROTEIN; ONCOPROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier32.65
Radius of gyration Rg (electron density) rg_electron33.09
Forward intensity I(0) i054057100.00
Molecular weight molecular_weight57902.0 kDa
Excluded volume excluded_volume72537 ų
Envelope volume envelope_volume90849 ų
Hydration-shell volume shell_volume25835 ų
Envelope diameter envelope_diameter126.6
Shell Rg shell_rg35.14
Envelope Rg envelope_rg33.47
Shape Rg shape_rg33.12
Total Rg total_rg33.18
Total atoms total_atoms4045
Residues n_residues524
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 dmax118.8
Rg (real space) rg_real33.35
Rg uncertainty (real space) rg_real_error1.41
I(0) (real space) i0_real5.4060e+07
I(0) uncertainty (real space) i0_real_error9.0470e+05
Rg (reciprocal space) rg_reciprocal33.06
I(0) (reciprocal space) i0_reciprocal54040000.0000
Solution quality estimate total_estimate0.7186
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.2
Skewness Skewness skewness0.649
Kurtosis Kurtosis kurtosis-0.311
Angular range angular_range— – 0.2450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha12020000.0000
Real-space data points n_real_points50
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.415; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.242; Smooth: 0.852

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)