9eq3

Structure of IgE HMM5 bound to FceRIa cryo-EM class 8

Method: ELECTRON MICROSCOPY Dmax: 184.4 Å Quality: GOOD

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

High affinity immunoglobulin epsilon receptor subunit alpha

Homo sapiens

UniProt P12319

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 5 其他Polymer 9 PDB declaration: pentameric(5) Consistent with protein copy count Chain R; UniProt 29–199 Not recorded IgE HMM5 heavy chain × 2 IgE HMM5 light chain × 2 ;alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 3 ;alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 4 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.90 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.

16 other PDB entries and 30 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FCERA_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain R; PDBConstruct 1–171; UniProt 29–199

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 9eq3

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9eq3
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9eq3
Deposition date deposition_date2024-03-20
Structure title titleStructure of IgE HMM5 bound to FceRIa cryo-EM class 8
Keywords keywordsIgE, Fc receptor, allergy, antibody, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier53.23
Radius of gyration Rg (electron density) rg_electron53.95
Forward intensity I(0) i0573054000.00
Molecular weight molecular_weight193350.0 kDa
Excluded volume excluded_volume240120 ų
Envelope volume envelope_volume369610 ų
Hydration-shell volume shell_volume63976 ų
Envelope diameter envelope_diameter194.7
Shell Rg shell_rg48.84
Envelope Rg envelope_rg53.18
Shape Rg shape_rg54.00
Total Rg total_rg53.61
Total atoms total_atoms13588
Residues n_residues1697
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 dmax184.4
Rg (real space) rg_real53.67
Rg uncertainty (real space) rg_real_error2.31
I(0) (real space) i0_real5.7310e+08
I(0) uncertainty (real space) i0_real_error1.2780e+07
Rg (reciprocal space) rg_reciprocal52.86
I(0) (reciprocal space) i0_reciprocal572400000.0000
Solution quality estimate total_estimate0.8239
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary49.2
Skewness Skewness skewness0.563
Kurtosis Kurtosis kurtosis-0.138
Angular range angular_range— – 0.1500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha37960000.0000
Real-space data points n_real_points31
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.795; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.944; Smooth: 0.377

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)