9mi6

Crystal structure of human FcRn in complex with nipocalimab Fab fragment

Method: X-RAY DIFFRACTION Dmax: 132.0 Å Quality: GOOD

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

IgG receptor FcRn large subunit p51

Homo sapiens

UniProt P55899

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 24–297 Not recorded Beta-2-microglobulin × 1 (P61769) nipocalimab Fab heavy chain × 1 nipocalimab Fab light chain × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;277.15 K;10% PEG 1000, 10% PEG 8000 Resolution 2.41 Å R-free 0.248

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.

30 other PDB entries and 70 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FCGRN_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–274; UniProt 24–297

Beta-2-microglobulin

Homo sapiens

UniProt P61769

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 B; UniProt 21–119 Not recorded IgG receptor FcRn large subunit p51 × 1 (P55899) nipocalimab Fab heavy chain × 1 nipocalimab Fab light chain × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;277.15 K;10% PEG 1000, 10% PEG 8000 Resolution 2.41 Å R-free 0.248

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.

1313 other PDB entries and 1998 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name B2MG_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–99; UniProt 21–119

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 9mi6

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9mi6
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9mi6
Deposition date deposition_date2024-12-12
Structure title titleCrystal structure of human FcRn in complex with nipocalimab Fab fragment
Keywords keywordsNEONATAL FC RECEPTOR, FCRN, INHIBITOR, BETA 2 MICROGLOBULIN, B2M, COMPLEX(ANTIBODY-ANTIGEN), IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier37.55
Radius of gyration Rg (electron density) rg_electron37.84
Forward intensity I(0) i0117299000.00
Molecular weight molecular_weight86126.0 kDa
Excluded volume excluded_volume107270 ų
Envelope volume envelope_volume147830 ų
Hydration-shell volume shell_volume35433 ų
Envelope diameter envelope_diameter134.7
Shell Rg shell_rg39.75
Envelope Rg envelope_rg37.93
Shape Rg shape_rg37.80
Total Rg total_rg38.11
Total atoms total_atoms6072
Residues n_residues792
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 dmax132.0
Rg (real space) rg_real38.05
Rg uncertainty (real space) rg_real_error1.43
I(0) (real space) i0_real1.1730e+08
I(0) uncertainty (real space) i0_real_error1.9880e+06
Rg (reciprocal space) rg_reciprocal37.75
I(0) (reciprocal space) i0_reciprocal117300000.0000
Solution quality estimate total_estimate0.8155
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary31.4
Skewness Skewness skewness0.556
Kurtosis Kurtosis kurtosis-0.415
Angular range angular_range— – 0.2100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha12100000.0000
Real-space data points n_real_points43
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.683; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.682; Smooth: 0.867

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)