7oit

Crystal structure of AP2 Mu2 in complex with FCHO2 WxxPhi motif (P3221 crystal form)

Method: X-RAY DIFFRACTION Dmax: 87.9 Å Quality: GOOD

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

AP-2 complex subunit mu

Rattus norvegicus

UniProt A0A140TAH5

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 157–434 Not recorded F-BAR domain only protein 2 × 1 (Q0JRZ9) GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;289 K;20mM Sodium formate; 20mM Ammonium acetate; 20mM Sodium citrate tribasic dihydrate; 20mM Sodium potassium tartrate tetrahydrate; 20mM Sodium oxamate, 100mM Imidazole MES monohydrate pH6.5 , 20% v/v Glycerol; 10% w/v PEG 4000 Resolution 1.65 Å R-free 0.202

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 A0A140TAH5_RAT
Isoform
PDB entities 1
Chains and sequence ranges Author chain AAA; PDBConstruct 8–285; UniProt 157–434

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 BBB; UniProt 422–432 Not recorded AP-2 complex subunit mu × 1 (A0A140TAH5) GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;289 K;20mM Sodium formate; 20mM Ammonium acetate; 20mM Sodium citrate tribasic dihydrate; 20mM Sodium potassium tartrate tetrahydrate; 20mM Sodium oxamate, 100mM Imidazole MES monohydrate pH6.5 , 20% v/v Glycerol; 10% w/v PEG 4000 Resolution 1.65 Å R-free 0.202

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 8 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 BBB; 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 7oit

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7oit
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id7oit
Deposition date deposition_date2021-05-12
Structure title titleCrystal structure of AP2 Mu2 in complex with FCHO2 WxxPhi motif (P3221 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_guinier24.15
Radius of gyration Rg (electron density) rg_electron23.59
Forward intensity I(0) i015512100.00
Molecular weight molecular_weight30867.0 kDa
Excluded volume excluded_volume39218 ų
Envelope volume envelope_volume47950 ų
Hydration-shell volume shell_volume18532 ų
Envelope diameter envelope_diameter88.5
Shell Rg shell_rg28.40
Envelope Rg envelope_rg24.04
Shape Rg shape_rg23.59
Total Rg total_rg24.27
Total atoms total_atoms2168
Residues n_residues268
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 dmax87.9
Rg (real space) rg_real24.47
Rg uncertainty (real space) rg_real_error0.81
I(0) (real space) i0_real1.5510e+07
I(0) uncertainty (real space) i0_real_error2.1430e+05
Rg (reciprocal space) rg_reciprocal24.40
I(0) (reciprocal space) i0_reciprocal15510000.0000
Solution quality estimate total_estimate0.7759
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.0
Skewness Skewness skewness0.613
Kurtosis Kurtosis kurtosis-0.184
Angular range angular_range— – 0.3300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4773000.0000
Real-space data points n_real_points65
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.556; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.454; Smooth: 0.959

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (2)

9. Files and Curves (10)