9ppp

Structure of Alpha Appendage of AP2 bound to the extended FxDxF motif derived of CCDC32

Method: X-RAY DIFFRACTION Dmax: 111.8 Å Quality: GOOD

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 695–938 Not recorded Coiled-coil domain-containing protein 32 × 1 (Q8BS39) 1PE PENTAETHYLENE GLYCOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;100 mM SPG pH 8.0, 25% PEG 1500 Resolution 2.10 Å R-free 0.205
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 695–938 Not recorded Coiled-coil domain-containing protein 32 × 1 (Q8BS39) 1PE PENTAETHYLENE GLYCOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;100 mM SPG pH 8.0, 25% PEG 1500 Resolution 2.10 Å R-free 0.205

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 25 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 1–244; UniProt 695–938 Author chain B; PDBConstruct 1–244; UniProt 695–938

Coiled-coil domain-containing protein 32

OrganismNot specified

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain P; UniProt 17–44 Not recorded AP-2 complex subunit alpha-2 × 1 (P17427) 1PE PENTAETHYLENE GLYCOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;100 mM SPG pH 8.0, 25% PEG 1500 Resolution 2.10 Å R-free 0.205
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain Q; UniProt 17–44 Not recorded AP-2 complex subunit alpha-2 × 1 (P17427) 1PE PENTAETHYLENE GLYCOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;100 mM SPG pH 8.0, 25% PEG 1500 Resolution 2.10 Å R-free 0.205

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 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CCD32_MOUSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain P; PDBConstruct 1–28; UniProt 17–44 Author chain Q; PDBConstruct 1–28; UniProt 17–44

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 9ppp

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9ppp
Deposition date deposition_date2025-07-21
Structure title titleStructure of Alpha Appendage of AP2 bound to the extended FxDxF motif derived of CCDC32
Keywords keywordsClathin, AP-2 adaptor complex, assembly chaperone, ENDOCYTOSIS; ENDOCYTOSIS
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier32.62
Radius of gyration Rg (electron density) rg_electron32.07
Forward intensity I(0) i058349800.00
Molecular weight molecular_weight60657.0 kDa
Excluded volume excluded_volume75958 ų
Envelope volume envelope_volume97099 ų
Hydration-shell volume shell_volume27475 ų
Envelope diameter envelope_diameter112.5
Shell Rg shell_rg35.99
Envelope Rg envelope_rg31.56
Shape Rg shape_rg32.05
Total Rg total_rg32.49
Total atoms total_atoms4264
Residues n_residues534
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 dmax111.8
Rg (real space) rg_real33.05
Rg uncertainty (real space) rg_real_error1.14
I(0) (real space) i0_real5.8350e+07
I(0) uncertainty (real space) i0_real_error1.0410e+06
Rg (reciprocal space) rg_reciprocal32.87
I(0) (reciprocal space) i0_reciprocal58340000.0000
Solution quality estimate total_estimate0.8107
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.4
Skewness Skewness skewness0.509
Kurtosis Kurtosis kurtosis-0.501
Angular range angular_range— – 0.2450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha10240000.0000
Real-space data points n_real_points50
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.727; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.587; Smooth: 0.765

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)