5lgk

Crystal structure of the human IgE-Fc bound to its B cell receptor derCD23

Method: X-RAY DIFFRACTION Dmax: 152.9 Å Quality: GOOD

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

Ig epsilon chain C region

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 × 3 其他Polymer 1 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 114–421 Chain B; UniProt 114–421 Not recorded Low affinity immunoglobulin epsilon Fc receptor × 1 (P06734) beta-D-mannopyranose-(1-4)-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 × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;294 K;15% (w/v) PEG 8,000, 0.1 M sodium citrate, 0.05 M ammonium sulfate Resolution 3.50 Å R-free 0.278
2 Other combination Heteromer Protein × 3 其他Polymer 1 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 114–421 Chain D; UniProt 114–421 Not recorded Low affinity immunoglobulin epsilon Fc receptor × 1 (P06734) beta-D-mannopyranose-(1-4)-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 × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;294 K;15% (w/v) PEG 8,000, 0.1 M sodium citrate, 0.05 M ammonium sulfate Resolution 3.50 Å R-free 0.278

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 50 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IGHE_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–307; UniProt 114–421 Author chain B; PDBConstruct 1–307; UniProt 114–421 Author chain C; PDBConstruct 1–307; UniProt 114–421 Author chain D; PDBConstruct 1–307; UniProt 114–421

Low affinity immunoglobulin epsilon Fc receptor

Homo sapiens

UniProt P06734

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 × 3 其他Polymer 1 PDB declaration: trimeric(3) Consistent with protein copy count Chain E; UniProt 165–284 Not recorded Ig epsilon chain C region × 2 (P01854) beta-D-mannopyranose-(1-4)-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 × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;294 K;15% (w/v) PEG 8,000, 0.1 M sodium citrate, 0.05 M ammonium sulfate Resolution 3.50 Å R-free 0.278
2 Other combination Heteromer Protein × 3 其他Polymer 1 PDB declaration: trimeric(3) Consistent with protein copy count Chain F; UniProt 165–284 Not recorded Ig epsilon chain C region × 2 (P01854) beta-D-mannopyranose-(1-4)-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 × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;294 K;15% (w/v) PEG 8,000, 0.1 M sodium citrate, 0.05 M ammonium sulfate Resolution 3.50 Å R-free 0.278

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.

22 other PDB entries and 78 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FCER2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain E; PDBConstruct 1–120; UniProt 165–284 Author chain F; PDBConstruct 1–120; UniProt 165–284

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 5lgk

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5lgk
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5lgk
Deposition date deposition_date2016-07-07
Structure title titleCrystal structure of the human IgE-Fc bound to its B cell receptor derCD23
Keywords keywordsIMMUNOGLOBULIN FOLD LECTIN, ANTIBODY RECEPTOR, 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_guinier43.98
Radius of gyration Rg (electron density) rg_electron43.93
Forward intensity I(0) i0424794000.00
Molecular weight molecular_weight162420.0 kDa
Excluded volume excluded_volume200760 ų
Envelope volume envelope_volume305690 ų
Hydration-shell volume shell_volume59731 ų
Envelope diameter envelope_diameter151.5
Shell Rg shell_rg46.92
Envelope Rg envelope_rg43.27
Shape Rg shape_rg43.92
Total Rg total_rg44.10
Total atoms total_atoms11420
Residues n_residues1432
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 dmax152.9
Rg (real space) rg_real44.18
Rg uncertainty (real space) rg_real_error1.64
I(0) (real space) i0_real4.2480e+08
I(0) uncertainty (real space) i0_real_error7.6430e+06
Rg (reciprocal space) rg_reciprocal43.98
I(0) (reciprocal space) i0_reciprocal424700000.0000
Solution quality estimate total_estimate0.8566
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary46.7
Skewness Skewness skewness0.463
Kurtosis Kurtosis kurtosis-0.344
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha45260000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.780; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.942; Smooth: 0.848

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 14 domains

CATH v4.4 (14 domains)

Domain ID domain_id5lgkA01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id5lgkA02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id5lgkA03
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id5lgkB01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id5lgkB02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id5lgkB03
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id5lgkC01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id5lgkC02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id5lgkC03
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id5lgkD01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id5lgkD02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id5lgkD03
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id5lgkE01
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology100 — Mannose-Binding Protein A; Chain A
Homologous superfamily homologous superfamily10 — Mannose-Binding Protein A, subunit A
Domain ID domain_id5lgkF01
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology100 — Mannose-Binding Protein A; Chain A
Homologous superfamily homologous superfamily10 — Mannose-Binding Protein A, subunit A

8. Citations (1)

9. Files and Curves (10)