7om8

Beta2 appendage domain of AP2 bound to terminal domains beneath the hub of the 28 triskelia mini clathrin coat complex, class 15

Method: ELECTRON MICROSCOPY Dmax: 114.7 Å Quality: GOOD

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

Clathrin heavy chain

OrganismNot specified

UniProt I3LGD4

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain Y; UniProt 1–299 Chain Z; UniProt 1–299 Not recorded AP-2 complex subunit beta × 1 (P63010) ELECTRON MICROSCOPY cryo-EM buffer:pH 6.4 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE;3 uL of sample applied to a grid and blotted for 4.5 s before plunging Resolution 10.50 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.

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

View Construct and Data Evidence
UniProt name I3LGD4_PIG
Isoform
PDB entities 1
Chains and sequence ranges Author chain Y; PDBConstruct 1–299; UniProt 1–299 Author chain Z; PDBConstruct 1–299; UniProt 1–299

AP-2 complex subunit beta

Homo sapiens

UniProt P63010

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 719–951 Not recorded Clathrin heavy chain × 2 (I3LGD4) ELECTRON MICROSCOPY cryo-EM buffer:pH 6.4 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE;3 uL of sample applied to a grid and blotted for 4.5 s before plunging Resolution 10.50 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.

21 other PDB entries and 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name AP2B1_HUMAN
Isoform P63010-2
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–233; UniProt 719–951

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 7om8

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7om8
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7om8
Deposition date deposition_date2021-05-21
Structure title titleBeta2 appendage domain of AP2 bound to terminal domains beneath the hub of the 28 triskelia mini clathrin coat complex, class 15
Keywords keywordsClathrin, clathrin adaptor, AP2, endocytosis; ENDOCYTOSIS
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier33.50
Radius of gyration Rg (electron density) rg_electron33.08
Forward intensity I(0) i057031800.00
Molecular weight molecular_weight60441.0 kDa
Excluded volume excluded_volume75980 ų
Envelope volume envelope_volume105040 ų
Hydration-shell volume shell_volume28215 ų
Envelope diameter envelope_diameter124.1
Shell Rg shell_rg37.20
Envelope Rg envelope_rg33.00
Shape Rg shape_rg33.08
Total Rg total_rg33.45
Total atoms total_atoms8456
Residues n_residues539
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 dmax114.7
Rg (real space) rg_real33.73
Rg uncertainty (real space) rg_real_error1.20
I(0) (real space) i0_real5.7030e+07
I(0) uncertainty (real space) i0_real_error9.7910e+05
Rg (reciprocal space) rg_reciprocal33.59
I(0) (reciprocal space) i0_reciprocal57020000.0000
Solution quality estimate total_estimate0.8336
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary31.7
Skewness Skewness skewness0.461
Kurtosis Kurtosis kurtosis-0.462
Angular range angular_range— – 0.2350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4622000.0000
Real-space data points n_real_points48
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.789; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.673; Smooth: 0.793

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)