7rwb

AP2 bound to the APA domain of SGIP in the presence of heparin

Method: ELECTRON MICROSCOPY Dmax: 207.7 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 × 8 PDB declaration: octameric(8) 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) 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 3.90 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 × 8 PDB declaration: octameric(8) 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) 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 3.90 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 × 8 PDB declaration: octameric(8) 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) 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 3.90 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 × 8 PDB declaration: octameric(8) 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) 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 3.90 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 7rwb

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7rwb
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id7rwb
Deposition date deposition_date2021-08-19
Structure title titleAP2 bound to the APA domain of SGIP in the presence of heparin
Keywords keywordsAP2, clathrin vesicle, endocytosis, lipid-binding, adaptor, membrane, transport, muniscin, regulator, SGIP1; ENDOCYTOSIS
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier59.08
Radius of gyration Rg (electron density) rg_electron59.08
Forward intensity I(0) i01544690000.00
Molecular weight molecular_weight338770.0 kDa
Excluded volume excluded_volume427350 ų
Envelope volume envelope_volume670420 ų
Hydration-shell volume shell_volume97185 ų
Envelope diameter envelope_diameter197.7
Shell Rg shell_rg59.37
Envelope Rg envelope_rg56.37
Shape Rg shape_rg59.08
Total Rg total_rg59.11
Total atoms total_atoms23962
Residues n_residues3408
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 dmax207.7
Rg (real space) rg_real59.15
Rg uncertainty (real space) rg_real_error1.90
I(0) (real space) i0_real1.5450e+09
I(0) uncertainty (real space) i0_real_error2.8220e+07
Rg (reciprocal space) rg_reciprocal58.98
I(0) (reciprocal space) i0_reciprocal1544000000.0000
Solution quality estimate total_estimate0.8051
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary61.5
Skewness Skewness skewness0.298
Kurtosis Kurtosis kurtosis-0.571
Angular range angular_range— – 0.1350 −1
Current regularization parameter α current_alpha0.0002
Highest regularization parameter α highest_alpha99400000.0000
Real-space data points n_real_points28
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.830; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.971; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 8 domains

CATH v4.4 (8 domains)

Domain ID domain_id7rwbA01
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology10 — Leucine-rich Repeat Variant
Homologous superfamily homologous superfamily10 — Leucine-rich Repeat Variant
Domain ID domain_id7rwbB01
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology10 — Leucine-rich Repeat Variant
Homologous superfamily homologous superfamily10 — Leucine-rich Repeat Variant
Domain ID domain_id7rwbM01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology450 — Beta-Lactamase
Homologous superfamily homologous superfamily60
Domain ID domain_id7rwbM02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1170 — Mu homology domain, subdomain B
Domain ID domain_id7rwba01
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology10 — Leucine-rich Repeat Variant
Homologous superfamily homologous superfamily10 — Leucine-rich Repeat Variant
Domain ID domain_id7rwbb01
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology10 — Leucine-rich Repeat Variant
Homologous superfamily homologous superfamily10 — Leucine-rich Repeat Variant
Domain ID domain_id7rwbm01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology450 — Beta-Lactamase
Homologous superfamily homologous superfamily60
Domain ID domain_id7rwbm02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1170 — Mu homology domain, subdomain B

8. Citations (1)

9. Files and Curves (10)