7oiq

Crystal structure of AP2 Mu2 in complex with FCHO2 WxxPhi motif (C2 crystal form)

Method: X-RAY DIFFRACTION Dmax: 87.4 Å Quality: EXCELLENT

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

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain AAA; UniProt 158–435 Not recorded F-BAR domain only protein 2 × 1 (Q0JRZ9) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;289 K;30mM Magnesium chloride hexahydrate, 30mM Calcium chloride dihydrate, 100mM Sodium HEPES MOPS (acid) pH 7.5, 20% v/v Ethylene glycol; 10 % w/v PEG 8000 Resolution 1.85 Å R-free 0.209
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain BBB; UniProt 158–435 Not recorded F-BAR domain only protein 2 × 1 (Q0JRZ9) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;289 K;30mM Magnesium chloride hexahydrate, 30mM Calcium chloride dihydrate, 100mM Sodium HEPES MOPS (acid) pH 7.5, 20% v/v Ethylene glycol; 10 % w/v PEG 8000 Resolution 1.85 Å R-free 0.209

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 46 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name AP2M1_RAT
Isoform
PDB entities 1
Chains and sequence ranges Author chain AAA; PDBConstruct 8–285; UniProt 158–435 Author chain BBB; PDBConstruct 8–285; UniProt 158–435

F-BAR domain only protein 2

Homo sapiens

UniProt Q0JRZ9

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 DDD; UniProt 422–432 Not recorded AP-2 complex subunit mu × 1 (P84092) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;289 K;30mM Magnesium chloride hexahydrate, 30mM Calcium chloride dihydrate, 100mM Sodium HEPES MOPS (acid) pH 7.5, 20% v/v Ethylene glycol; 10 % w/v PEG 8000 Resolution 1.85 Å R-free 0.209
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain CCC; UniProt 422–432 Not recorded AP-2 complex subunit mu × 1 (P84092) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;289 K;30mM Magnesium chloride hexahydrate, 30mM Calcium chloride dihydrate, 100mM Sodium HEPES MOPS (acid) pH 7.5, 20% v/v Ethylene glycol; 10 % w/v PEG 8000 Resolution 1.85 Å R-free 0.209

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 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FCHO2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain CCC; PDBConstruct 1–11; UniProt 422–432 Author chain DDD; PDBConstruct 1–11; UniProt 422–432

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 7oiq

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7oiq
Deposition date deposition_date2021-05-12
Structure title titleCrystal structure of AP2 Mu2 in complex with FCHO2 WxxPhi motif (C2 crystal form)
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_guinier28.44
Radius of gyration Rg (electron density) rg_electron27.75
Forward intensity I(0) i055743700.00
Molecular weight molecular_weight60557.0 kDa
Excluded volume excluded_volume77067 ų
Envelope volume envelope_volume100610 ų
Hydration-shell volume shell_volume30792 ų
Envelope diameter envelope_diameter90.8
Shell Rg shell_rg34.31
Envelope Rg envelope_rg27.87
Shape Rg shape_rg27.72
Total Rg total_rg28.59
Total atoms total_atoms4254
Residues n_residues528
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 dmax87.4
Rg (real space) rg_real28.36
Rg uncertainty (real space) rg_real_error0.52
I(0) (real space) i0_real5.5740e+07
I(0) uncertainty (real space) i0_real_error8.3240e+05
Rg (reciprocal space) rg_reciprocal28.39
I(0) (reciprocal space) i0_reciprocal55740000.0000
Solution quality estimate total_estimate0.9131
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary37.4
Skewness Skewness skewness0.176
Kurtosis Kurtosis kurtosis-0.634
Angular range angular_range— – 0.2800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha16010000.0000
Real-space data points n_real_points57
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.975; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.945

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (2)

9. Files and Curves (10)