7z5c

Chimera of AP2 with FCHO2 linker domain as a fusion on Cmu2 subunit

Method: ELECTRON MICROSCOPY Dmax: 123.5 Å Quality: EXCELLENT

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

AP-2 complex subunit alpha-2

Rattus norvegicus

UniProt P18484

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–620 Not recorded AP-2 complex subunit beta × 1 (P63010) AP-2 complex subunit mu × 1 (P84092) AP-2 complex subunit sigma × 1 (P62743) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6;50% HKT buffer (10mM Hepes, 10mM Tris 120mM potassium acetate pH 7.2) and 50% Core buffer (10mM Tris, 250mM NaCl, pH 8) cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.16 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.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name AP2A2_RAT
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–621; UniProt 1–620

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 1–591 Not recorded AP-2 complex subunit alpha-2 × 1 (P18484) AP-2 complex subunit mu × 1 (P84092) AP-2 complex subunit sigma × 1 (P62743) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6;50% HKT buffer (10mM Hepes, 10mM Tris 120mM potassium acetate pH 7.2) and 50% Core buffer (10mM Tris, 250mM NaCl, pH 8) cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.16 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
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–591; UniProt 1–591

AP-2 complex subunit mu

Rattus norvegicus

UniProt P84092

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain M; UniProt 1–435 Not recorded AP-2 complex subunit alpha-2 × 1 (P18484) AP-2 complex subunit beta × 1 (P63010) AP-2 complex subunit sigma × 1 (P62743) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6;50% HKT buffer (10mM Hepes, 10mM Tris 120mM potassium acetate pH 7.2) and 50% Core buffer (10mM Tris, 250mM NaCl, pH 8) cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.16 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.

35 other PDB entries and 47 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name AP2M1_RAT
Isoform
PDB entities 3
Chains and sequence ranges 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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain S; UniProt 1–142 Not recorded AP-2 complex subunit alpha-2 × 1 (P18484) AP-2 complex subunit beta × 1 (P63010) AP-2 complex subunit mu × 1 (P84092) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6;50% HKT buffer (10mM Hepes, 10mM Tris 120mM potassium acetate pH 7.2) and 50% Core buffer (10mM Tris, 250mM NaCl, pH 8) cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.16 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

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 7z5c

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7z5c
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7z5c
Deposition date deposition_date2022-03-09
Structure title titleChimera of AP2 with FCHO2 linker domain as a fusion on Cmu2 subunit
Keywords keywordsadaptor complex, AP2, trafficking, clathrin, CCP, PROTEIN TRANSPORT; PROTEIN TRANSPORT
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier39.84
Radius of gyration Rg (electron density) rg_electron38.95
Forward intensity I(0) i0533448000.00
Molecular weight molecular_weight194970.0 kDa
Excluded volume excluded_volume246910 ų
Envelope volume envelope_volume329840 ų
Hydration-shell volume shell_volume68180 ų
Envelope diameter envelope_diameter125.0
Shell Rg shell_rg46.89
Envelope Rg envelope_rg38.20
Shape Rg shape_rg38.94
Total Rg total_rg39.46
Total atoms total_atoms13707
Residues n_residues1717
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 dmax123.5
Rg (real space) rg_real39.56
Rg uncertainty (real space) rg_real_error0.92
I(0) (real space) i0_real5.3340e+08
I(0) uncertainty (real space) i0_real_error9.0360e+06
Rg (reciprocal space) rg_reciprocal39.74
I(0) (reciprocal space) i0_reciprocal533500000.0000
Solution quality estimate total_estimate0.9046
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary52.5
Skewness Skewness skewness0.092
Kurtosis Kurtosis kurtosis-0.602
Angular range angular_range— – 0.2000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha145700000.0000
Real-space data points n_real_points41
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.943; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.988; Smooth: 0.940

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)