9dva

F-actin binding interface of alpha-E-catenin ABD (cadherin-catenin complex) and afadin

Method: ELECTRON MICROSCOPY Dmax: 173.9 Å Quality: GOOD

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

Actin, alpha skeletal muscle

OrganismNot specified

UniProt P68139

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 3–377 Chain B; UniProt 3–377 Chain C; UniProt 3–377 Chain D; UniProt 3–377 Chain E; UniProt 3–377 Non-standard monomer:Yes (specific site not provided by mmCIF) Catenin alpha-1 × 2 (P26231) Afadin × 1 (Q9QZQ1) 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

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.

57 other PDB entries and 66 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ACTS_CHICK
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–375; UniProt 3–377 Author chain B; PDBConstruct 1–375; UniProt 3–377 Author chain C; PDBConstruct 1–375; UniProt 3–377 Author chain D; PDBConstruct 1–375; UniProt 3–377 Author chain E; PDBConstruct 1–375; UniProt 3–377

Catenin alpha-1

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain F; UniProt 1–906 Chain H; UniProt 1–906 Not recorded Actin, alpha skeletal muscle × 5 (P68139) Afadin × 1 (Q9QZQ1) 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

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 CTNA1_MOUSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain F; PDBConstruct 1–906; UniProt 1–906 Author chain H; PDBConstruct 1–906; UniProt 1–906

Afadin

Mus musculus

UniProt Q9QZQ1

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain G; UniProt 1393–1602 Not recorded Actin, alpha skeletal muscle × 5 (P68139) Catenin alpha-1 × 2 (P26231) 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

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.

4 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name AFAD_MOUSE
Isoform
PDB entities 3
Chains and sequence ranges Author chain G; PDBConstruct 10–219; UniProt 1393–1602

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 9dva

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9dva
Deposition date deposition_date2024-10-07
最后修订 last_revision2024-10-30
Structure title titleF-actin binding interface of alpha-E-catenin ABD (cadherin-catenin complex) and afadin
Keywords keywordsCytoskeleton, cell adhesion, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier48.28
Radius of gyration Rg (electron density) rg_electron48.43
Forward intensity I(0) i01041080000.00
Molecular weight molecular_weight264730.0 kDa
Excluded volume excluded_volume330280 ų
Envelope volume envelope_volume463710 ų
Hydration-shell volume shell_volume80979 ų
Envelope diameter envelope_diameter188.3
Shell Rg shell_rg51.22
Envelope Rg envelope_rg48.10
Shape Rg shape_rg48.44
Total Rg total_rg48.48
Total atoms total_atoms18529
Residues n_residues2349
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 dmax173.9
Rg (real space) rg_real48.51
Rg uncertainty (real space) rg_real_error1.93
I(0) (real space) i0_real1.0410e+09
I(0) uncertainty (real space) i0_real_error2.2350e+07
Rg (reciprocal space) rg_reciprocal48.28
I(0) (reciprocal space) i0_reciprocal1041000000.0000
Solution quality estimate total_estimate0.8500
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary52.7
Skewness Skewness skewness0.483
Kurtosis Kurtosis kurtosis-0.178
Angular range angular_range— – 0.1650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha149700000.0000
Real-space data points n_real_points34
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.716; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.981; Smooth: 0.916

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)