3cm9

Solution Structure of Human SIgA2

Method: SOLUTION SCATTERING Dmax: 236.7 Å Quality: GOOD

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

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 heavy chain × 4 Immunoglobulin light chain × 4 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 2, 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 3cm9

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3cm9
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id3cm9
Deposition date deposition_date2008-03-21
Structure title titleSolution Structure of Human SIgA2
Keywords keywords;Secretory IgA2; Secretory IgA1; IgA; mucosal immunity; X-ray and neutron scattering; constrained modelling, 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_guinier83.03
Radius of gyration Rg (electron density) rg_electron83.06
Forward intensity I(0) i0191856000000.00
Molecular weight molecular_weight3684100.0 kDa
Excluded volume excluded_volume4469800 ų
Envelope volume envelope_volume961800 ų
Hydration-shell volume shell_volume108960 ų
Envelope diameter envelope_diameter267.0
Shell Rg shell_rg70.58
Envelope Rg envelope_rg73.56
Shape Rg shape_rg83.22
Total Rg total_rg83.04
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 dmax236.7
Rg (real space) rg_real82.28
Rg uncertainty (real space) rg_real_error1.29
I(0) (real space) i0_real1.9040e+11
I(0) uncertainty (real space) i0_real_error3.7110e+09
Rg (reciprocal space) rg_reciprocal81.33
I(0) (reciprocal space) i0_reciprocal190900000000.0000
Solution quality estimate total_estimate0.8478
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary99.7
Skewness Skewness skewness0.275
Kurtosis Kurtosis kurtosis-0.563
Angular range angular_range— – 0.0950 −1
Current regularization parameter α current_alpha0.0651
Highest regularization parameter α highest_alpha60420000.0000
Real-space data points n_real_points20
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.992; Stabil: 0.994; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.031

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (3)

9. Files and Curves (10)