9pwb

Structure of AP-2 bound to the dileucine motif of CCDC32; combined map

Method: ELECTRON MICROSCOPY Dmax: 119.0 Å Quality: EXCELLENT

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

AP-2 complex subunit alpha-2

Mus musculus

UniProt P17427

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 9–620 Not recorded AP-2 complex subunit beta × 1 (Q9DBG3) Coiled-coil domain-containing protein 32 × 1 (Q8BS39) AP-2 complex subunit mu × 1 (P84091) AP-2 complex subunit sigma × 1 (P62744) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 2.64 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.

23 other PDB entries and 26 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name AP2A2_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–613; UniProt 9–620

AP-2 complex subunit beta

Mus musculus

UniProt Q9DBG3

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain B; UniProt 26–582 Not recorded AP-2 complex subunit alpha-2 × 1 (P17427) Coiled-coil domain-containing protein 32 × 1 (Q8BS39) AP-2 complex subunit mu × 1 (P84091) AP-2 complex subunit sigma × 1 (P62744) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 2.64 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.

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

View Construct and Data Evidence
UniProt name AP2B1_MOUSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–557; UniProt 26–582

Coiled-coil domain-containing protein 32

Mus musculus

UniProt Q8BS39

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain C; UniProt 151–161 Not recorded AP-2 complex subunit alpha-2 × 1 (P17427) AP-2 complex subunit beta × 1 (Q9DBG3) AP-2 complex subunit mu × 1 (P84091) AP-2 complex subunit sigma × 1 (P62744) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 2.64 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.

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

View Construct and Data Evidence
UniProt name CCD32_MOUSE
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–11; UniProt 151–161

AP-2 complex subunit mu

Mus musculus

UniProt P84091

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain M; UniProt 1–135 Not recorded AP-2 complex subunit alpha-2 × 1 (P17427) AP-2 complex subunit beta × 1 (Q9DBG3) Coiled-coil domain-containing protein 32 × 1 (Q8BS39) AP-2 complex subunit sigma × 1 (P62744) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 2.64 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.

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

View Construct and Data Evidence
UniProt name AP2M1_MOUSE
Isoform
PDB entities 4
Chains and sequence ranges Author chain M; PDBConstruct 1–135; UniProt 1–135

AP-2 complex subunit sigma

Mus musculus

UniProt P62744

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain S; UniProt 1–141 Not recorded AP-2 complex subunit alpha-2 × 1 (P17427) AP-2 complex subunit beta × 1 (Q9DBG3) Coiled-coil domain-containing protein 32 × 1 (Q8BS39) AP-2 complex subunit mu × 1 (P84091) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 2.64 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 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name AP2S1_RAT
Isoform
PDB entities 5
Chains and sequence ranges Author chain S; PDBConstruct 1–141; UniProt 1–141

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 9pwb

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9pwb
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id9pwb
Deposition date deposition_date2025-08-04
Structure title titleStructure of AP-2 bound to the dileucine motif of CCDC32; combined map
Keywords keywordsClathin, AP-2 adaptor complex, CCDC32, assembly chaperone, ENDOCYTOSIS; ENDOCYTOSIS
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier38.99
Radius of gyration Rg (electron density) rg_electron38.16
Forward intensity I(0) i0387571000.00
Molecular weight molecular_weight165260.0 kDa
Excluded volume excluded_volume209200 ų
Envelope volume envelope_volume281720 ų
Hydration-shell volume shell_volume60406 ų
Envelope diameter envelope_diameter123.9
Shell Rg shell_rg45.54
Envelope Rg envelope_rg37.00
Shape Rg shape_rg38.13
Total Rg total_rg38.70
Total atoms total_atoms11620
Residues n_residues1457
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 dmax119.0
Rg (real space) rg_real38.73
Rg uncertainty (real space) rg_real_error0.61
I(0) (real space) i0_real3.8760e+08
I(0) uncertainty (real space) i0_real_error6.3840e+06
Rg (reciprocal space) rg_reciprocal38.89
I(0) (reciprocal space) i0_reciprocal387600000.0000
Solution quality estimate total_estimate0.9085
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary52.3
Skewness Skewness skewness0.052
Kurtosis Kurtosis kurtosis-0.680
Angular range angular_range— – 0.2050 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha96520000.0000
Real-space data points n_real_points42
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.959; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.991; Smooth: 0.937

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)