7sht

Structure of a partially disrupted IgE high affinity receptor complex bound to an omalizumab variant

Method: ELECTRON MICROSCOPY Dmax: 133.9 Å Quality: REASONABLE

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 × 7 其他Polymer 4 PDB declaration: heptameric(7) Consistent with protein copy count Chain A; UniProt 30–197 Fragment:extracellular portion Mutation:W156C Immunoglobulin heavy constant epsilon × 2 (P01854) clone_7 Variable fragment heavy chain × 2 clone_7 Variable fragment light chain × 2 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 × 1 ;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 ; × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 7.29 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 1
Chains and sequence ranges Author chain A; PDBConstruct 30–197; UniProt 30–197

Immunoglobulin heavy constant epsilon

Homo sapiens

UniProt P01854

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 × 7 其他Polymer 4 PDB declaration: heptameric(7) Consistent with protein copy count Chain B; UniProt 109–428 Chain D; UniProt 109–428 Mutation:G335C High affinity immunoglobulin epsilon receptor subunit alpha × 1 (P12319) clone_7 Variable fragment heavy chain × 2 clone_7 Variable fragment light chain × 2 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 × 1 ;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 ; × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 7.29 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.

33 other PDB entries and 51 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IGHE_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 3–322; UniProt 109–428 Author chain D; PDBConstruct 3–322; UniProt 109–428

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 7sht

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7sht
Deposition date deposition_date2021-10-11
Structure title titleStructure of a partially disrupted IgE high affinity receptor complex bound to an omalizumab variant
Keywords keywordsIgE, allergy, Xolair, Omalizumab, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier40.53
Radius of gyration Rg (electron density) rg_electron40.06
Forward intensity I(0) i0329599000.00
Molecular weight molecular_weight142940.0 kDa
Excluded volume excluded_volume177000 ų
Envelope volume envelope_volume263470 ų
Hydration-shell volume shell_volume56436 ų
Envelope diameter envelope_diameter142.3
Shell Rg shell_rg44.86
Envelope Rg envelope_rg38.33
Shape Rg shape_rg40.06
Total Rg total_rg40.35
Total atoms total_atoms10062
Residues n_residues1259
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 dmax133.9
Rg (real space) rg_real40.42
Rg uncertainty (real space) rg_real_error1.24
I(0) (real space) i0_real3.2960e+08
I(0) uncertainty (real space) i0_real_error6.3660e+06
Rg (reciprocal space) rg_reciprocal40.53
I(0) (reciprocal space) i0_reciprocal329600000.0000
Solution quality estimate total_estimate0.6683
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary54.9
Skewness Skewness skewness0.184
Kurtosis Kurtosis kurtosis-0.403
Angular range angular_range— – 0.1950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha34110000.0000
Real-space data points n_real_points40
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.884; Stabil: 1.000; Sysdev: 0.025; Positv: 1.000; Valcen: 0.999; Smooth: 0.957

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)