9ofr

CRYSTAL STRUCTURE OF THE HUMAN IGA1 FC FRAGMENT-FC-ALPHA RECEPTOR (CD89) COMPLEX

Method: X-RAY DIFFRACTION Dmax: 168.5 Å Quality: GOOD

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 Other combination Heteromer Protein × 4 其他Polymer 1 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 123–335 Chain B; UniProt 123–335 Fragment:FC fragment, UNP residues 123-335 Immunoglobulin alpha Fc receptor × 2 (P24071) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 7 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;294 K;0.15M sodium chloride 0.1M Tris-HCl pH 8.0 8% PEG 6000 Resolution 2.65 Å R-free 0.264
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain E; UniProt 123–335 Chain G; UniProt 123–335 Fragment:FC fragment, UNP residues 123-335 Immunoglobulin alpha Fc receptor × 2 (P24071) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 7 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;294 K;0.15M sodium chloride 0.1M Tris-HCl pH 8.0 8% PEG 6000 Resolution 2.65 Å R-free 0.264

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 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IGHA1_HUMAN
Isoform P01876-1
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–214; UniProt 123–335 Author chain B; PDBConstruct 2–214; UniProt 123–335 Author chain E; PDBConstruct 2–214; UniProt 123–335 Author chain G; PDBConstruct 2–214; UniProt 123–335

Immunoglobulin alpha Fc receptor

Homo sapiens

UniProt P24071

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 4 其他Polymer 1 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 22–216 Chain D; UniProt 22–216 Not recorded Isoform 1 of Immunoglobulin heavy constant alpha 1 × 2 (P01876) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 7 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;294 K;0.15M sodium chloride 0.1M Tris-HCl pH 8.0 8% PEG 6000 Resolution 2.65 Å R-free 0.264
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain F; UniProt 22–216 Chain H; UniProt 22–216 Not recorded Isoform 1 of Immunoglobulin heavy constant alpha 1 × 2 (P01876) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 7 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;294 K;0.15M sodium chloride 0.1M Tris-HCl pH 8.0 8% PEG 6000 Resolution 2.65 Å R-free 0.264

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.

5 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FCAR_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–195; UniProt 22–216 Author chain D; PDBConstruct 1–195; UniProt 22–216 Author chain F; PDBConstruct 1–195; UniProt 22–216 Author chain H; PDBConstruct 1–195; UniProt 22–216

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 9ofr

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9ofr
Deposition date deposition_date2025-04-30
最后修订 last_revision2026-05-06
Structure title titleCRYSTAL STRUCTURE OF THE HUMAN IGA1 FC FRAGMENT-FC-ALPHA RECEPTOR (CD89) COMPLEX
Keywords keywordsIMMUNOGLOBULIN, IGA1, IMMUNE SYSTEM, IMMUNOGLOBULIN-LIKE BETA SANDWICH, FC FRAGMENT, FC ALPHA RECEPTOR, CD89; IMMUNE SYSTEM
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier47.94
Radius of gyration Rg (electron density) rg_electron48.08
Forward intensity I(0) i0497249000.00
Molecular weight molecular_weight183350.0 kDa
Excluded volume excluded_volume229520 ų
Envelope volume envelope_volume354710 ų
Hydration-shell volume shell_volume64993 ų
Envelope diameter envelope_diameter181.0
Shell Rg shell_rg48.16
Envelope Rg envelope_rg47.34
Shape Rg shape_rg48.10
Total Rg total_rg48.05
Total atoms total_atoms12908
Residues n_residues1624
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 dmax168.5
Rg (real space) rg_real48.11
Rg uncertainty (real space) rg_real_error1.90
I(0) (real space) i0_real4.9720e+08
I(0) uncertainty (real space) i0_real_error1.0110e+07
Rg (reciprocal space) rg_reciprocal47.94
I(0) (reciprocal space) i0_reciprocal497100000.0000
Solution quality estimate total_estimate0.8515
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary56.2
Skewness Skewness skewness0.458
Kurtosis Kurtosis kurtosis0.044
Angular range angular_range— – 0.1650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha20280000.0000
Real-space data points n_real_points34
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.735; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.860

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)