1iga

MODEL OF HUMAN IGA1 DETERMINED BY SOLUTION SCATTERING CURVE-FITTING AND HOMOLOGY MODELLING

Method: SOLUTION SCATTERING Dmax: 219.2 Å Quality: REASONABLE

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

IGA1

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 1–353 Chain B; UniProt 1–353 Fragment:CHAINS A AND B, HEAVY, CHAINS C AND D, LIGHT 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 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IGHA1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 123–475; UniProt 1–353 Author chain B; PDBConstruct 123–475; UniProt 1–353

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 1iga

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1iga
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id1iga
Deposition date deposition_date1998-12-23
Structure title titleMODEL OF HUMAN IGA1 DETERMINED BY SOLUTION SCATTERING CURVE-FITTING AND HOMOLOGY MODELLING
Keywords keywordsIMMUNOGLOBULIN, IGA1; IMMUNOGLOBULIN
Experimental Method methodSOLUTION SCATTERING

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

Radius of gyration Rg (Guinier) rg_guinier71.78
Radius of gyration Rg (electron density) rg_electron73.02
Forward intensity I(0) i0326788000.00
Molecular weight molecular_weight148430.0 kDa
Excluded volume excluded_volume180030 ų
Envelope volume envelope_volume233560 ų
Hydration-shell volume shell_volume34760 ų
Envelope diameter envelope_diameter233.9
Shell Rg shell_rg49.15
Envelope Rg envelope_rg68.39
Shape Rg shape_rg72.93
Total Rg total_rg72.48
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 dmax219.2
Rg (real space) rg_real72.28
Rg uncertainty (real space) rg_real_error2.07
I(0) (real space) i0_real3.2620e+08
I(0) uncertainty (real space) i0_real_error7.5380e+06
Rg (reciprocal space) rg_reciprocal68.42
I(0) (reciprocal space) i0_reciprocal324100000.0000
Solution quality estimate total_estimate0.6454
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks4
Primary peak position r_peak_primary29.9
Skewness Skewness skewness0.508
Kurtosis Kurtosis kurtosis-0.600
Angular range angular_range— – 0.1100 −1
Current regularization parameter α current_alpha0.0033
Highest regularization parameter α highest_alpha7943000.0000
Real-space data points n_real_points23
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.190; Stabil: 0.993; Sysdev: 1.000; Positv: 1.000; Valcen: 0.478; Smooth: 0.356

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (3)

9. Files and Curves (10)