4gi0

Crystal structure of CD23 lectin domain mutant E249A

Method: X-RAY DIFFRACTION Dmax: 90.5 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 homooligomer Homooligomer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 156–298 Chain B; UniProt 156–298 Chain C; UniProt 156–298 Fragment:UNP residues 156-298 Mutation:E249A GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;291 K;0.2M potassium thiocyanate, 0.1M bis tris propane pH 8.5, 20% PEG 3350, VAPOR DIFFUSION, SITTING DROP, temperature 291K Resolution 2.27 Å R-free 0.251

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 79 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 Author chain B; PDBConstruct 1–143; UniProt 156–298 Author chain C; 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 4gi0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4gi0
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4gi0
Deposition date deposition_date2012-08-08
Structure title titleCrystal structure of CD23 lectin domain mutant E249A
Keywords keywordsReceptor, 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_guinier27.64
Radius of gyration Rg (electron density) rg_electron27.03
Forward intensity I(0) i038946800.00
Molecular weight molecular_weight45629.0 kDa
Excluded volume excluded_volume55856 ų
Envelope volume envelope_volume72957 ų
Hydration-shell volume shell_volume23704 ų
Envelope diameter envelope_diameter97.9
Shell Rg shell_rg32.46
Envelope Rg envelope_rg26.91
Shape Rg shape_rg27.03
Total Rg total_rg27.61
Total atoms total_atoms3203
Residues n_residues400
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 dmax90.5
Rg (real space) rg_real27.66
Rg uncertainty (real space) rg_real_error0.81
I(0) (real space) i0_real3.8950e+07
I(0) uncertainty (real space) i0_real_error6.0380e+05
Rg (reciprocal space) rg_reciprocal27.66
I(0) (reciprocal space) i0_reciprocal38950000.0000
Solution quality estimate total_estimate0.8013
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks4
Primary peak position r_peak_primary22.2
Skewness Skewness skewness0.224
Kurtosis Kurtosis kurtosis-0.680
Angular range angular_range— – 0.2850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha11450000.0000
Real-space data points n_real_points58
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.845; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.883; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd4gi0a_
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.169.1.0 — automated matches
Domain ID domain_idd4gi0b_
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.169.1.0 — automated matches
Domain ID domain_idd4gi0c_
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.169.1.0 — automated matches

CATH v4.4 (3 domains)

Domain ID domain_id4gi0A01
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_id4gi0B01
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_id4gi0C01
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)