1f2q

CRYSTAL STRUCTURE OF THE HUMAN HIGH-AFFINITY IGE RECEPTOR

Method: X-RAY DIFFRACTION Dmax: 61.4 Å Quality: REASONABLE

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

HIGH AFFINITY IMMUNOGLOBULIN EPSILON RECEPTOR ALPHA-SUBUNIT

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 Monomer Protein × 1 其他Polymer 2 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 26–201 Fragment:EXTRACELLULAR DOMAIN 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 × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.5;297 K;PEG 4000, Tris, Sodium Acetate, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 297K Resolution 2.40 Å R-free 0.254

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 FCEA_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–176; UniProt 26–201

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 1f2q

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1f2q
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1f2q
Deposition date deposition_date2000-05-28
Structure title titleCRYSTAL STRUCTURE OF THE HUMAN HIGH-AFFINITY IGE RECEPTOR
Keywords keywordsImmunoglobulin Fold, Glycoprotein, Receptor, IgE-binding Protein, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier18.75
Radius of gyration Rg (electron density) rg_electron17.79
Forward intensity I(0) i08166680.00
Molecular weight molecular_weight20723.0 kDa
Excluded volume excluded_volume25823 ų
Envelope volume envelope_volume32161 ų
Hydration-shell volume shell_volume15522 ų
Envelope diameter envelope_diameter61.1
Shell Rg shell_rg23.33
Envelope Rg envelope_rg18.10
Shape Rg shape_rg17.77
Total Rg total_rg18.81
Total atoms total_atoms1463
Residues n_residues167
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 dmax61.4
Rg (real space) rg_real18.70
Rg uncertainty (real space) rg_real_error0.41
I(0) (real space) i0_real8.1670e+06
I(0) uncertainty (real space) i0_real_error1.0760e+05
Rg (reciprocal space) rg_reciprocal18.71
I(0) (reciprocal space) i0_reciprocal8167000.0000
Solution quality estimate total_estimate0.7370
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary21.0
Skewness Skewness skewness0.211
Kurtosis Kurtosis kurtosis-0.479
Angular range angular_range— – 0.4250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1950000.0000
Real-space data points n_real_points74
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.898; Stabil: 1.000; Sysdev: 0.313; Positv: 1.000; Valcen: 0.994; Smooth: 0.950

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1f2qa1
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.4 — I set domains
Domain ID domain_idd1f2qa2
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.4 — I set domains

CATH v4.4 (2 domains)

Domain ID domain_id1f2qA01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id1f2qA02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)