4j6q

Crystal structure of calcium2+-free wild-type CD23 lectin domain (crystal form G)

Method: X-RAY DIFFRACTION Dmax: 52.4 Å Quality: GOOD

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

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 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 156–298 Fragment:Soluble head domain of the B-cell receptor CD23 (UNP Residues 156-298) No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 4.5;298 K;3.7 M NaCl and 0.1 M citric acid pH 4.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K Resolution 2.54 Å R-free 0.239
2 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 156–298 Fragment:Soluble head domain of the B-cell receptor CD23 (UNP Residues 156-298) No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 4.5;298 K;3.7 M NaCl and 0.1 M citric acid pH 4.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K Resolution 2.54 Å R-free 0.239

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 1
Chains and sequence ranges Author chain A; 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 4j6q

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4j6q
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4j6q
Deposition date deposition_date2013-02-11
Structure title titleCrystal structure of calcium2+-free wild-type CD23 lectin domain (crystal form G)
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_guinier15.28
Radius of gyration Rg (electron density) rg_electron14.25
Forward intensity I(0) i04962670.00
Molecular weight molecular_weight15156.0 kDa
Excluded volume excluded_volume18542 ų
Envelope volume envelope_volume20458 ų
Hydration-shell volume shell_volume12308 ų
Envelope diameter envelope_diameter51.8
Shell Rg shell_rg19.93
Envelope Rg envelope_rg14.77
Shape Rg shape_rg14.22
Total Rg total_rg15.40
Total atoms total_atoms1064
Residues n_residues132
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 dmax52.4
Rg (real space) rg_real15.22
Rg uncertainty (real space) rg_real_error0.30
I(0) (real space) i0_real4.9630e+06
I(0) uncertainty (real space) i0_real_error5.5910e+04
Rg (reciprocal space) rg_reciprocal15.22
I(0) (reciprocal space) i0_reciprocal4963000.0000
Solution quality estimate total_estimate0.8573
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary19.9
Skewness Skewness skewness0.279
Kurtosis Kurtosis kurtosis-0.166
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha959400.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.729; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.990; Smooth: 0.963

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd4j6qa_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.169 — C-type lectin-like
Superfamily Superfamily superfamilyd.169.1 — C-type lectin-like
Family Family familyd.169.1.1 — C-type lectin domain

CATH v4.4 (1 domains)

Domain ID domain_id4j6qA01
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)