9r2e

Structure of ARGX-121 Fab fragment in complex with the Fc fragment of IgA1

Method: X-RAY DIFFRACTION Dmax: 176.0 Å Quality: REASONABLE

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

Isoform 1 of Immunoglobulin heavy constant alpha 1

Homo sapiens

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain P; UniProt 123–335 Chain Q; UniProt 123–335 Not recorded ARGX-121 Fab fragment heavy chain × 2 ARGX-121 Fab fragment light chain × 2 EDO 1,2-ETHANEDIOL × 4 PEG DI(HYDROXYETHYL)ETHER × 5 MG MAGNESIUM ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277 K;16% (w/v) PEG8000, 20% (v/v) Glycerol, 0.16 M MgAcetate, 0.08 M Na Cacodylate pH 6.50 Resolution 2.54 Å R-free 0.252

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 P01876-1
PDB entities 3
Chains and sequence ranges Author chain P; PDBConstruct 1–213; UniProt 123–335 Author chain Q; PDBConstruct 1–213; UniProt 123–335

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 9r2e

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9r2e
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id9r2e
Deposition date deposition_date2025-04-30
最后修订 last_revision2025-05-14
Structure title titleStructure of ARGX-121 Fab fragment in complex with the Fc fragment of IgA1
Keywords keywordsAntibody, immune system, IgA mediated autoimmunity, immunoglobulin, PROTEROS BIOSTRUCTURES GMBH; IMMUNE SYSTEM
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier48.93
Radius of gyration Rg (electron density) rg_electron50.11
Forward intensity I(0) i0286749000.00
Molecular weight molecular_weight137470.0 kDa
Excluded volume excluded_volume171460 ų
Envelope volume envelope_volume250300 ų
Hydration-shell volume shell_volume47226 ų
Envelope diameter envelope_diameter187.3
Shell Rg shell_rg45.26
Envelope Rg envelope_rg50.30
Shape Rg shape_rg50.04
Total Rg total_rg50.11
Total atoms total_atoms9665
Residues n_residues1283
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 dmax176.0
Rg (real space) rg_real49.92
Rg uncertainty (real space) rg_real_error2.31
I(0) (real space) i0_real2.8670e+08
I(0) uncertainty (real space) i0_real_error5.3650e+06
Rg (reciprocal space) rg_reciprocal48.94
I(0) (reciprocal space) i0_reciprocal286400000.0000
Solution quality estimate total_estimate0.5274
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary38.5
Skewness Skewness skewness0.643
Kurtosis Kurtosis kurtosis-0.116
Angular range angular_range— – 0.1600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha17180000.0000
Real-space data points n_real_points33
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.650; Stabil: 1.000; Sysdev: 0.013; Positv: 1.000; Valcen: 0.528; Smooth: 0.335

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)