7oi5

Crystal structure of AP2 Mu2 - FCHO2 chimera (GST cleaved)

Method: X-RAY DIFFRACTION Dmax: 118.3 Å Quality: GOOD

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

AP-2 complex subunit mu,F-BAR domain only protein 2

Homo sapiens

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 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 158–435 Not recorded GOL GLYCEROL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 9.1;289 K;20% w/v PEG 3350, 0.2 M Sodium phosphate dibasic dehydrate pH 9.1. The crystal was cryo-protected by soaking in mother liquor supplemented with 25% glycerol. Resolution 2.61 Å R-free 0.297
2 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain D; UniProt 158–435 Not recorded GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 9.1;289 K;20% w/v PEG 3350, 0.2 M Sodium phosphate dibasic dehydrate pH 9.1. The crystal was cryo-protected by soaking in mother liquor supplemented with 25% glycerol. Resolution 2.61 Å R-free 0.297

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 B; PDBConstruct 6–283; UniProt 158–435 Author chain D; PDBConstruct 6–283; UniProt 158–435

AP-2 complex subunit mu,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 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 316–351 Not recorded GOL GLYCEROL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 9.1;289 K;20% w/v PEG 3350, 0.2 M Sodium phosphate dibasic dehydrate pH 9.1. The crystal was cryo-protected by soaking in mother liquor supplemented with 25% glycerol. Resolution 2.61 Å R-free 0.297
2 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain D; UniProt 316–351 Not recorded GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 9.1;289 K;20% w/v PEG 3350, 0.2 M Sodium phosphate dibasic dehydrate pH 9.1. The crystal was cryo-protected by soaking in mother liquor supplemented with 25% glycerol. Resolution 2.61 Å R-free 0.297

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 1
Chains and sequence ranges Author chain B; PDBConstruct 324–359; UniProt 316–351 Author chain D; PDBConstruct 324–359; UniProt 316–351

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 7oi5

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7oi5
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7oi5
Deposition date deposition_date2021-05-11
Structure title titleCrystal structure of AP2 Mu2 - FCHO2 chimera (GST cleaved)
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_guinier33.67
Radius of gyration Rg (electron density) rg_electron33.41
Forward intensity I(0) i066180300.00
Molecular weight molecular_weight66267.0 kDa
Excluded volume excluded_volume83945 ų
Envelope volume envelope_volume115890 ų
Hydration-shell volume shell_volume31074 ų
Envelope diameter envelope_diameter124.9
Shell Rg shell_rg36.61
Envelope Rg envelope_rg33.75
Shape Rg shape_rg33.47
Total Rg total_rg33.49
Total atoms total_atoms4653
Residues n_residues573
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 dmax118.3
Rg (real space) rg_real33.95
Rg uncertainty (real space) rg_real_error1.35
I(0) (real space) i0_real6.6180e+07
I(0) uncertainty (real space) i0_real_error1.0600e+06
Rg (reciprocal space) rg_reciprocal33.78
I(0) (reciprocal space) i0_reciprocal66170000.0000
Solution quality estimate total_estimate0.8199
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary32.7
Skewness Skewness skewness0.559
Kurtosis Kurtosis kurtosis-0.088
Angular range angular_range— – 0.2350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha10370000.0000
Real-space data points n_real_points48
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.775; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.655; Smooth: 0.676

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id7oi5B01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1170 — Mu homology domain, subdomain B
Domain ID domain_id7oi5D01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1170 — Mu homology domain, subdomain B

8. Citations (2)

9. Files and Curves (10)