2qtj

Solution structure of human dimeric immunoglobulin A

Method: SOLUTION SCATTERING Dmax: 253.9 Å Quality: GOOD

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

Ig alpha-1 chain C region

OrganismNot specified

UniProt P01876

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–475 Chain B; UniProt 1–475 Not recorded Kappa light chain IgA1 × 2 SOLUTION SCATTERING mmCIF provides none of the parsed experimental conditions Resolution not provided
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 1–475 Chain D; UniProt 1–475 Not recorded Kappa light chain IgA1 × 2 SOLUTION SCATTERING mmCIF provides none of the parsed experimental conditions Resolution not provided

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.

14 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IGHA1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 1–475; UniProt 1–475 Author chain B; PDBConstruct 1–475; UniProt 1–475 Author chain C; PDBConstruct 1–475; UniProt 1–475 Author chain D; PDBConstruct 1–475; UniProt 1–475

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 2qtj

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2qtj
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2qtj
Deposition date deposition_date2007-08-02
Structure title titleSolution structure of human dimeric immunoglobulin A
Keywords keywords;X-ray and neutron solution scattering, immunology, antibody, immunoglobulin A1, Chromophore, Glycoprotein, Immunoglobulin C region, Immunoglobulin domain, IMMUNE SYSTEM ;; IMMUNE SYSTEM
Experimental Method methodSOLUTION SCATTERING

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

Radius of gyration Rg (Guinier) rg_guinier97.68
Radius of gyration Rg (electron density) rg_electron98.56
Forward intensity I(0) i0124231000000.00
Molecular weight molecular_weight2968600.0 kDa
Excluded volume excluded_volume3600600 ų
Envelope volume envelope_volume1727900 ų
Hydration-shell volume shell_volume135930 ų
Envelope diameter envelope_diameter303.7
Shell Rg shell_rg91.68
Envelope Rg envelope_rg99.99
Shape Rg shape_rg98.65
Total Rg total_rg98.55
Total atoms total_atoms
Residues n_residues
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 dmax253.9
Rg (real space) rg_real94.20
Rg uncertainty (real space) rg_real_error1.23
I(0) (real space) i0_real1.2030e+11
I(0) uncertainty (real space) i0_real_error2.6820e+09
Rg (reciprocal space) rg_reciprocal92.00
I(0) (reciprocal space) i0_reciprocal121900000000.0000
Solution quality estimate total_estimate0.8939
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary95.2
Skewness Skewness skewness0.288
Kurtosis Kurtosis kurtosis-0.809
Angular range angular_range— – 0.0800 −1
Current regularization parameter α current_alpha0.1864
Highest regularization parameter α highest_alpha62780000.0000
Real-space data points n_real_points17
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.810; Stabil: 0.922; Sysdev: 1.000; Positv: 1.000; Valcen: 0.879; Smooth: 0.555

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)