3chn

Solution structure of human secretory IgA1

Method: SOLUTION SCATTERING Dmax: 239.7 Å Quality: EXCELLENT

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain A; UniProt 1–353 Chain B; UniProt 1–353 Chain C; UniProt 1–353 Chain D; UniProt 1–353 Not recorded Immunoglobulin kappa light chain × 4 Secretory component × 1 (P01833) Secretory component × 1 (P01833) 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 17 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 123–475; UniProt 1–353 Author chain B; PDBConstruct 123–475; UniProt 1–353 Author chain C; PDBConstruct 123–475; UniProt 1–353 Author chain D; PDBConstruct 123–475; UniProt 1–353

Secretory component

OrganismNot specified

UniProt P01833

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain J; UniProt 353–458 Chain S; UniProt 19–603 Fragment:Ig-like V-type domain 4 Immunoglobulin kappa light chain × 4 Ig alpha-1 chain C region × 4 (P01876) 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.

15 other PDB entries and 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PIGR_HUMAN
Isoform
PDB entities 3, 4
Chains and sequence ranges Author chain J; PDBConstruct 1–106; UniProt 353–458 Author chain S; PDBConstruct 1–585; UniProt 19–603

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 3chn

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3chn
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3chn
Deposition date deposition_date2008-03-10
Structure title titleSolution structure of human secretory IgA1
Keywords keywords;Immunoglobulin A, Secretory immunoglobulin A, Mucosal immunity, neutron scattering, X-ray scattering, Chromophore, Glycoprotein, Immunoglobulin C region, Immunoglobulin domain, Membrane, Phosphoprotein, Secreted, Transmembrane, IMMUNE SYSTEM ;; IMMUNE SYSTEM
Experimental Method methodSOLUTION SCATTERING

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

Radius of gyration Rg (Guinier) rg_guinier89.50
Radius of gyration Rg (electron density) rg_electron89.86
Forward intensity I(0) i0195871000000.00
Molecular weight molecular_weight3729900.0 kDa
Excluded volume excluded_volume4526600 ų
Envelope volume envelope_volume952620 ų
Hydration-shell volume shell_volume101280 ų
Envelope diameter envelope_diameter275.8
Shell Rg shell_rg71.27
Envelope Rg envelope_rg80.11
Shape Rg shape_rg90.09
Total Rg total_rg89.83
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 dmax239.7
Rg (real space) rg_real85.99
Rg uncertainty (real space) rg_real_error0.92
I(0) (real space) i0_real1.8850e+11
I(0) uncertainty (real space) i0_real_error3.7710e+09
Rg (reciprocal space) rg_reciprocal86.78
I(0) (reciprocal space) i0_reciprocal194200000000.0000
Solution quality estimate total_estimate0.9105
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary112.8
Skewness Skewness skewness0.171
Kurtosis Kurtosis kurtosis-0.736
Angular range angular_range— – 0.0850 −1
Current regularization parameter α current_alpha0.9160
Highest regularization parameter α highest_alpha49890000.0000
Real-space data points n_real_points18
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.999; Stabil: 0.967; Sysdev: 1.000; Positv: 1.000; Valcen: 0.946; Smooth: 0.001

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (4)

9. Files and Curves (10)