4gko

Crystal structure of the calcium2+-bound human IgE-Fc(epsilon)3-4 bound to its B cell receptor derCD23

Method: X-RAY DIFFRACTION Dmax: 178.3 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 × 4 其他Polymer 2 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 209–428 Chain B; UniProt 209–428 Fragment:UNP residues 209-428 Low affinity immunoglobulin epsilon Fc receptor × 2 (P06734) ;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 ; × 2 CA CALCIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;291 K;0.2 M sodium acetate trihydrate, 0.1 M Tris pH 8.5, 16% PEG 4000, 10 mM CaCl2, VAPOR DIFFUSION, SITTING DROP, temperature 291K Resolution 3.30 Å R-free 0.312
2 Other combination Heteromer Protein × 4 其他Polymer 2 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 209–428 Chain D; UniProt 209–428 Fragment:UNP residues 209-428 Low affinity immunoglobulin epsilon Fc receptor × 2 (P06734) ;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 ; × 2 MAN alpha-D-mannopyranose × 2 CA CALCIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;291 K;0.2 M sodium acetate trihydrate, 0.1 M Tris pH 8.5, 16% PEG 4000, 10 mM CaCl2, VAPOR DIFFUSION, SITTING DROP, temperature 291K Resolution 3.30 Å R-free 0.312
3 Other combination Heteromer Protein × 4 其他Polymer 2 PDB declaration: tetrameric(4) Consistent with protein copy count Chain E; UniProt 209–428 Chain F; UniProt 209–428 Fragment:UNP residues 209-428 Low affinity immunoglobulin epsilon Fc receptor × 2 (P06734) ;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 ; × 2 CA CALCIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;291 K;0.2 M sodium acetate trihydrate, 0.1 M Tris pH 8.5, 16% PEG 4000, 10 mM CaCl2, VAPOR DIFFUSION, SITTING DROP, temperature 291K Resolution 3.30 Å R-free 0.312

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 49 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 4–223; UniProt 209–428 Author chain B; PDBConstruct 4–223; UniProt 209–428 Author chain C; PDBConstruct 4–223; UniProt 209–428 Author chain D; PDBConstruct 4–223; UniProt 209–428 Author chain E; PDBConstruct 4–223; UniProt 209–428 Author chain F; PDBConstruct 4–223; UniProt 209–428

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 × 4 其他Polymer 2 PDB declaration: tetrameric(4) Consistent with protein copy count Chain G; UniProt 156–298 Chain H; UniProt 156–298 Fragment:UNP residues 156-298 Ig epsilon chain C region × 2 (P01854) ;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 ; × 2 CA CALCIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;291 K;0.2 M sodium acetate trihydrate, 0.1 M Tris pH 8.5, 16% PEG 4000, 10 mM CaCl2, VAPOR DIFFUSION, SITTING DROP, temperature 291K Resolution 3.30 Å R-free 0.312
2 Other combination Heteromer Protein × 4 其他Polymer 2 PDB declaration: tetrameric(4) Consistent with protein copy count Chain I; UniProt 156–298 Chain J; UniProt 156–298 Fragment:UNP residues 156-298 Ig epsilon chain C region × 2 (P01854) ;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 ; × 2 MAN alpha-D-mannopyranose × 2 CA CALCIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;291 K;0.2 M sodium acetate trihydrate, 0.1 M Tris pH 8.5, 16% PEG 4000, 10 mM CaCl2, VAPOR DIFFUSION, SITTING DROP, temperature 291K Resolution 3.30 Å R-free 0.312
3 Other combination Heteromer Protein × 4 其他Polymer 2 PDB declaration: tetrameric(4) Consistent with protein copy count Chain K; UniProt 156–298 Chain L; UniProt 156–298 Fragment:UNP residues 156-298 Ig epsilon chain C region × 2 (P01854) ;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 ; × 2 CA CALCIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;291 K;0.2 M sodium acetate trihydrate, 0.1 M Tris pH 8.5, 16% PEG 4000, 10 mM CaCl2, VAPOR DIFFUSION, SITTING DROP, temperature 291K Resolution 3.30 Å R-free 0.312

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 77 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 G; PDBConstruct 1–143; UniProt 156–298 Author chain H; PDBConstruct 1–143; UniProt 156–298 Author chain I; PDBConstruct 1–143; UniProt 156–298 Author chain J; PDBConstruct 1–143; UniProt 156–298 Author chain K; PDBConstruct 1–143; UniProt 156–298 Author chain L; PDBConstruct 1–143; UniProt 156–298

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 4gko

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4gko
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4gko
Deposition date deposition_date2012-08-13
Structure title titleCrystal structure of the calcium2+-bound human IgE-Fc(epsilon)3-4 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_guinier53.22
Radius of gyration Rg (electron density) rg_electron53.01
Forward intensity I(0) i0831280000.00
Molecular weight molecular_weight230830.0 kDa
Excluded volume excluded_volume285230 ų
Envelope volume envelope_volume458560 ų
Hydration-shell volume shell_volume74360 ų
Envelope diameter envelope_diameter184.3
Shell Rg shell_rg54.28
Envelope Rg envelope_rg51.03
Shape Rg shape_rg53.00
Total Rg total_rg53.08
Total atoms total_atoms16214
Residues n_residues1987
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 dmax178.3
Rg (real space) rg_real53.15
Rg uncertainty (real space) rg_real_error1.69
I(0) (real space) i0_real8.3130e+08
I(0) uncertainty (real space) i0_real_error1.6170e+07
Rg (reciprocal space) rg_reciprocal53.26
I(0) (reciprocal space) i0_reciprocal831400000.0000
Solution quality estimate total_estimate0.8742
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary65.4
Skewness Skewness skewness0.214
Kurtosis Kurtosis kurtosis-0.369
Angular range angular_range— – 0.1500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha25540000.0000
Real-space data points n_real_points31
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.859; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.791

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 18 domains

CATH v4.4 (18 domains)

Domain ID domain_id4gkoA01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id4gkoA02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id4gkoB01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id4gkoB02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id4gkoC01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id4gkoC02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id4gkoD01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id4gkoD02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id4gkoE01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id4gkoE02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id4gkoF01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id4gkoF02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id4gkoG01
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_id4gkoH01
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_id4gkoI01
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_id4gkoJ01
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_id4gkoK01
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_id4gkoL01
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)