7ohi

FCHO1-peptide-AP2 alpha ear complex

Method: X-RAY DIFFRACTION Dmax: 76.4 Å Quality: REASONABLE

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 F-BAR domain only protein 1 × 1 (O14526) SO4 SULFATE ION × 5 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;289 K;1.6M Magnesium sulfate heptahydrate 0.1M MES pH 6.5. The crystal were subsequently cryo-protected with ~20% glycerol final. Resolution 1.41 Å R-free 0.215

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 7–250; UniProt 695–938

F-BAR domain only protein 1

OrganismNot specified

UniProt O14526

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 B; UniProt 426–448 Not recorded AP-2 complex subunit alpha-2 × 1 (P17427) SO4 SULFATE ION × 5 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;289 K;1.6M Magnesium sulfate heptahydrate 0.1M MES pH 6.5. The crystal were subsequently cryo-protected with ~20% glycerol final. Resolution 1.41 Å R-free 0.215

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name FCHO1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–23; UniProt 426–448

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 7ohi

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7ohi
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7ohi
Deposition date deposition_date2021-05-11
Structure title titleFCHO1-peptide-AP2 alpha ear complex
Keywords keywordsclathrin-mediated endocytosis (CME), protein recycling, plasma membrane, ENDOCYTOSIS; ENDOCYTOSIS
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.91
Radius of gyration Rg (electron density) rg_electron21.10
Forward intensity I(0) i016439900.00
Molecular weight molecular_weight30267.0 kDa
Excluded volume excluded_volume37776 ų
Envelope volume envelope_volume45308 ų
Hydration-shell volume shell_volume18756 ų
Envelope diameter envelope_diameter79.0
Shell Rg shell_rg26.88
Envelope Rg envelope_rg21.53
Shape Rg shape_rg21.10
Total Rg total_rg21.92
Total atoms total_atoms4220
Residues n_residues264
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 dmax76.4
Rg (real space) rg_real22.02
Rg uncertainty (real space) rg_real_error0.51
I(0) (real space) i0_real1.6440e+07
I(0) uncertainty (real space) i0_real_error2.2660e+05
Rg (reciprocal space) rg_reciprocal22.00
I(0) (reciprocal space) i0_reciprocal16440000.0000
Solution quality estimate total_estimate0.6195
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.8
Skewness Skewness skewness0.485
Kurtosis Kurtosis kurtosis-0.193
Angular range angular_range— – 0.3650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4086000.0000
Real-space data points n_real_points68
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.737; Stabil: 1.000; Sysdev: 0.000; Positv: 1.000; Valcen: 0.841; Smooth: 0.998

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (2)

9. Files and Curves (10)