7rwa

AP2 bound to heparin and Tgn38 tyrosine cargo peptide

Method: ELECTRON MICROSCOPY Dmax: 197.9 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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain A; UniProt 1–620 Chain a; UniProt 1–620 Not recorded AP-2 complex subunit beta × 2 (Q9DBG3) AP-2 complex subunit mu × 2 (P84091) AP-2 complex subunit sigma × 2 (P62743) Trans-Golgi network integral membrane protein TGN38 peptide × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE;Blot force -10, 4 second blot, 4 uL sample Resolution 4.70 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 1–621; UniProt 1–620 Author chain a; PDBConstruct 1–621; UniProt 1–620

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain B; UniProt 1–591 Chain b; UniProt 1–591 Not recorded AP-2 complex subunit alpha-2 × 2 (P17427) AP-2 complex subunit mu × 2 (P84091) AP-2 complex subunit sigma × 2 (P62743) Trans-Golgi network integral membrane protein TGN38 peptide × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE;Blot force -10, 4 second blot, 4 uL sample Resolution 4.70 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 1–591; UniProt 1–591 Author chain b; PDBConstruct 1–591; UniProt 1–591

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain M; UniProt 1–435 Chain m; UniProt 1–435 Not recorded AP-2 complex subunit alpha-2 × 2 (P17427) AP-2 complex subunit beta × 2 (Q9DBG3) AP-2 complex subunit sigma × 2 (P62743) Trans-Golgi network integral membrane protein TGN38 peptide × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE;Blot force -10, 4 second blot, 4 uL sample Resolution 4.70 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 3
Chains and sequence ranges Author chain M; PDBConstruct 1–435; UniProt 1–435 Author chain m; PDBConstruct 1–435; UniProt 1–435

AP-2 complex subunit sigma

Mus musculus

UniProt P62743

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain S; UniProt 1–142 Chain s; UniProt 1–142 Not recorded AP-2 complex subunit alpha-2 × 2 (P17427) AP-2 complex subunit beta × 2 (Q9DBG3) AP-2 complex subunit mu × 2 (P84091) Trans-Golgi network integral membrane protein TGN38 peptide × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE;Blot force -10, 4 second blot, 4 uL sample Resolution 4.70 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 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name AP2S1_MOUSE
Isoform
PDB entities 4
Chains and sequence ranges Author chain S; PDBConstruct 1–142; UniProt 1–142 Author chain s; PDBConstruct 1–142; UniProt 1–142

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 7rwa

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7rwa
Deposition date deposition_date2021-08-19
Structure title titleAP2 bound to heparin and Tgn38 tyrosine cargo peptide
Keywords keywordsAP2, clathrin vesicle, endocytosis, lipid-binding, adaptor, membrane, transport, cargo; ENDOCYTOSIS
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier56.68
Radius of gyration Rg (electron density) rg_electron56.69
Forward intensity I(0) i01100680000.00
Molecular weight molecular_weight226020.0 kDa
Excluded volume excluded_volume260600 ų
Envelope volume envelope_volume623210 ų
Hydration-shell volume shell_volume95399 ų
Envelope diameter envelope_diameter189.8
Shell Rg shell_rg57.71
Envelope Rg envelope_rg52.98
Shape Rg shape_rg56.69
Total Rg total_rg56.72
Total atoms total_atoms16158
Residues n_residues3244
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 dmax197.9
Rg (real space) rg_real59.15
Rg uncertainty (real space) rg_real_error0.94
I(0) (real space) i0_real1.1030e+09
I(0) uncertainty (real space) i0_real_error2.0500e+07
Rg (reciprocal space) rg_reciprocal56.68
I(0) (reciprocal space) i0_reciprocal1101000000.0000
Solution quality estimate total_estimate0.6715
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary70.7
Skewness Skewness skewness0.477
Kurtosis Kurtosis kurtosis-0.089
Angular range angular_range— – 0.1400 −1
Current regularization parameter α current_alpha1.1270
Highest regularization parameter α highest_alpha96310000.0000
Real-space data points n_real_points29
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.798; Stabil: 0.877; Sysdev: 0.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.733

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)