SAXSdb — 6o3e

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

Catenin alpha-1

Mus musculus

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 82–883 Chain B； UniProt 82–883	Mutation：C116S	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 8.5；295 K；50 mM Tris, pH 8.5, 60 mM lithium sulfate, 23.5 % PEG 400	Resolution 4.00 Å R-free 0.243

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.

Other PDB	Difference from Current Entry 6O3E	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1DOV CRYSTAL STRUCTURE OF THE ALPHA-CATENIN DIMERIZATION DOMAIN Deposited 1999-12-21	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 82–262（181 aa） Fragment：DIMERIZATION DOMAIN	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.9；295 K；PEG 400, Tris, urea, dithiothreitol, pH 8.9, VAPOR DIFFUSION, HANGING DROP, temperature 295K	Resolution 3.00 Å R-free 0.263
1DOV CRYSTAL STRUCTURE OF THE ALPHA-CATENIN DIMERIZATION DOMAIN Deposited 1999-12-21	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 82–262（181 aa） Fragment：DIMERIZATION DOMAIN	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.9；295 K；PEG 400, Tris, urea, dithiothreitol, pH 8.9, VAPOR DIFFUSION, HANGING DROP, temperature 295K	Resolution 3.00 Å R-free 0.263
1DOW CRYSTAL STRUCTURE OF A CHIMERA OF BETA-CATENIN AND ALPHA-CATENIN Deposited 1999-12-21	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 57–261（205 aa） Fragment：DIMERIZATION AND BETA-CATENIN BINDING REGION	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	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
4E17 Alpha-E-catenin is an autoinhibited molecule that co-activates vinculin Deposited 2012-03-05	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 321–356（36 aa） Fragment：vinculin binding domain (UNP residues 321-356)	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.8；283 K；20% PEG8000, 100 mM MES, pH 6.8, 3 mM DTT, VAPOR DIFFUSION, HANGING DROP, temperature 283K	Resolution 2.30 Å R-free 0.240
4E18 Alpha-E-catenin is an autoinhibited molecule that co-activates vinculin Deposited 2012-03-05	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 302–356（55 aa） Fragment：vinculin binding domain (UNP residues 302-356)	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；22% PEG3350, 100 mM bis-tris-propane, pH 8.0, 100 mM sodium nitrate, 3 mM DTT, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.40 Å R-free 0.273
4K1N Crystal structure of full-length mouse alphaE-catenin Deposited 2013-04-05	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–906（906 aa） Chain B 1–906（906 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；293 K；0.2 M Sodium Citrate, 20% (w/v) PEG-3350, vapor diffusion, temperature 293K	Resolution 6.50 Å R-free 0.247
5Y04 Crystal Structure of the complex between the vinculin D1 domain and alphaE-catenin Deposited 2017-07-14	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 276–375（100 aa） Fragment：UNP RESIDUES 276-375	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 8；293 K；100MM IMIDAZOLE, 0.5-0.7M POTASSIUM TARTRATE, 0.35M SODIUM FORMATE	Resolution 2.85 Å R-free 0.281
6DV1 Crystal structure of the alpha-E-catenin actin-binding domain Deposited 2018-06-22	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 652–906（255 aa） Chain B 652–906（255 aa）	Not recorded	BR BROMIDE ION × 5 SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；0.2 M potassium bromide, 2.2 M ammonium sulfate, 3% w/v D-galactose	Resolution 2.20 Å R-free 0.252
6WVT Structural basis of alphaE-catenin - F-actin catch bond behavior Deposited 2020-05-06	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain K 671–906（236 aa） Chain L 671–906（236 aa） Chain N 671–906（236 aa） Chain O 671–906（236 aa） Chain Q 671–906（236 aa） Chain X 671–906（236 aa）	Not recorded	MG MAGNESIUM ION × 6 ADP ADENOSINE-5'-DIPHOSPHATE × 6	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.56 Å
9DVA F-actin binding interface of alpha-E-catenin ABD (cadherin-catenin complex) and afadin Deposited 2024-10-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain F 1–906（906 aa） Chain H 1–906（906 aa）	Not recorded	ADP ADENOSINE-5'-DIPHOSPHATE × 5 MG MAGNESIUM ION × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.10 Å

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

View Construct and Data Evidence

UniProt name	CTNA1_MOUSE
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 5–806； UniProt 82–883 Author chain B； PDBConstruct 5–806； UniProt 82–883

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	6o3e
Deposition date deposition_date	2019-02-26
Structure title title	mouse aE-catenin 82-883
Keywords keywords	catenin, cell adhesion, actin binding; CELL ADHESION
Experimental Method method	X-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier	39.70 Å
Radius of gyration Rg (electron density) rg_electron	39.48 Å
Forward intensity I(0) i0	215417000.00
Molecular weight molecular_weight	115070.0 kDa
Excluded volume excluded_volume	142760 Å³
Envelope volume envelope_volume	207000 Å³
Hydration-shell volume shell_volume	45385 Å³
Envelope diameter envelope_diameter	136.5 Å
Shell Rg shell_rg	43.51 Å
Envelope Rg envelope_rg	38.27 Å
Shape Rg shape_rg	39.52 Å
Total Rg total_rg	39.61 Å
Total atoms total_atoms	8070
Residues n_residues	1077
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	133.0 Å
Rg (real space) rg_real	39.71 Å
Rg uncertainty (real space) rg_real_error	1.32 Å
I(0) (real space) i0_real	2.1540e+08
I(0) uncertainty (real space) i0_real_error	3.8180e+06
Rg (reciprocal space) rg_reciprocal	39.71 Å
I(0) (reciprocal space) i0_reciprocal	215400000.0000
Solution quality estimate total_estimate	0.8918
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	49.9 Å
Skewness Skewness skewness	0.282
Kurtosis Kurtosis kurtosis	-0.403
Angular range angular_range	— – 0.2000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	11140000.0000
Real-space data points n_real_points	41
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.900; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.987; Smooth: 0.903

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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8. Citations (1)

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Unit-cell length a length_a	145.262 Å
Unit-cell length b length_b	145.262 Å
Unit-cell length c length_c	136.269 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	120.00 °
Molecules per unit cell Z z_pdb	6

Space group space_group	P 32
Space-group number int_tables_number	145
Crystal system crystal_system	—

Resolution resolution	4.001 Å
Low-resolution limit resolution_low	19.971 Å
R factor r_factor	0.2150
R_work r_work	0.2135
R_free r_free	0.2429

Description description	Catenin alpha-1
Molecular weight formula_weight	89068.4 kDa
Mutation mutation	C116S
Source method src_method	man
Copy count entity_count	2

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	8070

mouse aE-catenin 82-883

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

Catenin alpha-1

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

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

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (1)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

来源生物 organism	Mus musculus
通用名 common_name	Mouse
NCBI Class编号 ncbi_taxonomy_id	10090
宿主生物 host_organism	Escherichia coli

fit	/app/data/saxs_computation/o3/6o3e/6o3e.fit
pddf	/app/data/pr_computation/o3/6o3e/6o3e.pr.out
profile	/app/data/saxs_computation/o3/6o3e/6o3e.dat