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3se4

human IFNw-IFNAR ternary complex

Method: X-RAY DIFFRACTION Dmax: 106.9 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Interferon alpha/beta receptor 1

Homo sapiens

UniProt P17181

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 × 3 PDB declaration: trimeric（3） Consistent with protein copy count Chain A； UniProt 28–436 Fragment：IFNw (UNP Residues 28-436) Mutation：N101Q Interferon omega-1 × 1 （P05000） Interferon alpha/beta receptor 2 × 1 （P48551） NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions：pH 6.5；293 K；19% (w/v) PEG 3350, 100 mM Ammonium sulfate, 100 mM Bis-Tris pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 3.50 Å R-free 0.288

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.

Other PDB Difference from Current Entry 3SE4 Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
3S98 human IFNAR1 Deposited 2011-06-01 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 30–332（303 aa） Fragment：UNP Residues 30-332
Non-standard monomer：Yes (specific site not provided by mmCIF) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION
X-ray crystallization conditions 298 K；20% (w/v) PEG 3350, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 1.90 Å R-free 0.234
3SE3 human IFNa2-IFNAR ternary complex Deposited 2011-06-10 Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain A 28–436（409 aa） Fragment：IFNa2(YNS) (UNP Residues 28-436)
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5；293 K；15% (w/v) PEG 3350, 100 mM Na malonate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 4.00 Å R-free 0.311
4PO6 Crystal structure of the human TYK2 FERM and SH2 domains with an IFNAR1 intracellular peptide Deposited 2014-02-25 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 478–507（30 aa） Fragment：unp residues 475-507
Not recorded GOL GLYCEROL × 3 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7；293 K；0.1 M Tris HCl pH 7.0, 0.2 M MgCl2, and 8-12% PEG 8000, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 1.99 Å R-free 0.234
8Y31 The crystal structure of the QX006N-Fab/IFNAR1-SD123 complex Deposited 2024-01-28 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain E 1–333（333 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION, RECRYSTALLIZATION；289 K；8%(w/v) PEG3350 50 mM Na-Citrate pH 5.5, 100 mM (NH4)2Citrate, 250 mM NaCl, 5 mM Hexadecyltrimethylammonium Bromide
Resolution 2.68 Å R-free 0.239
8Y31 The crystal structure of the QX006N-Fab/IFNAR1-SD123 complex Deposited 2024-01-28 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain F 1–333（333 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION, RECRYSTALLIZATION；289 K；8%(w/v) PEG3350 50 mM Na-Citrate pH 5.5, 100 mM (NH4)2Citrate, 250 mM NaCl, 5 mM Hexadecyltrimethylammonium Bromide
Resolution 2.68 Å R-free 0.239

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

View Construct and Data Evidence
UniProt name INAR1_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 6–414； UniProt 28–436

Interferon omega-1

Homo sapiens

UniProt P05000

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 × 3 PDB declaration: trimeric（3） Consistent with protein copy count Chain B； UniProt 22–195 Fragment：UNP Residues 22-195 Interferon alpha/beta receptor 1 × 1 （P17181） Interferon alpha/beta receptor 2 × 1 （P48551） NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions：pH 6.5；293 K；19% (w/v) PEG 3350, 100 mM Ammonium sulfate, 100 mM Bis-Tris pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 3.50 Å R-free 0.288

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name IFNW1_HUMAN
Isoform —
PDB entities 2
Chains and sequence ranges Author chain B； PDBConstruct 4–177； UniProt 22–195

Interferon alpha/beta receptor 2

Homo sapiens

UniProt P48551

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 × 3 PDB declaration: trimeric（3） Consistent with protein copy count Chain C； UniProt 34–232 Fragment：UNP Residues 34-232 Interferon alpha/beta receptor 1 × 1 （P17181） Interferon omega-1 × 1 （P05000） NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions：pH 6.5；293 K；19% (w/v) PEG 3350, 100 mM Ammonium sulfate, 100 mM Bis-Tris pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 3.50 Å R-free 0.288

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.

Other PDB Difference from Current Entry 3SE4 Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1N6U NMR structure of the interferon-binding ectodomain of the human interferon receptor Deposited 2002-11-12 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 28–237（210 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 8；308 K；Ionic strength (raw mmCIF value) 20mM Tris；Pressure ambient
NMR measurement conditions pH 8；308 K；Ionic strength (raw mmCIF value) 20mM Tris；Pressure ambient
NMR measurement conditions pH 8；305 K；Ionic strength (raw mmCIF value) 20mM Tris；Pressure ambient
NMR sample composition 0.5mM IFNAR2-EC U-15N; 20mM d-Tris pH 8, 0.02% NaN3; | 95% H2O/5% D2O
NMR sample composition 0.35mM IFNAR2-EC U-15N,13C; 20mM d-Tris pH 8, 0.02% NaN3; | 95% H2O/5% D2O
NMR sample composition 0.35mM IFNAR2-EC U-15N,13C; 20mM d-Tris pH 8, 0.02% NaN3; | 99% D2O
Resolution not provided
1N6V Average structure of the interferon-binding ectodomain of the human type I interferon receptor Deposited 2002-11-12 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 28–237（210 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 8；308 K；Ionic strength (raw mmCIF value) 20mM Tris buffer；Pressure ambient
NMR measurement conditions pH 8；308 K；Ionic strength (raw mmCIF value) 20mM Tris buffer；Pressure ambient
NMR measurement conditions pH 8；305 K；Ionic strength (raw mmCIF value) 20mM Tris buffer；Pressure ambient
NMR sample composition 0.4mM U-15N IFNAR2-EC; 20mM d-Tris pH 8, 0.02% NaN3 | 95% H2O/5% D2O
NMR sample composition 0.35mM U-13C,15N IFNAR2-EC; 20mM d-Tris pH 8, 0.02% NaN3 | 95% H2O/5% D2O
NMR sample composition 0.3mM U-13C,15N IFNAR2-EC; 20mM d-Tris pH 8, 0.02% NaN3 | 99% D2O
Resolution not provided
2LAG Structure of the 44 kDa complex of interferon-alpha2 with the extracellular part of IFNAR2 obtained by 2D-double difference NOESY Deposited 2011-03-13 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 28–239（212 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 8；305 K；Ionic strength (raw mmCIF value) 25；Pressure ambient
NMR sample composition 0.25 mM [U-99% 2H] Interferon alpha/beta receptor 2, 0.25 mM [U-99% 2H] Interferon alpha-2, 100% D2O | 100% D2O
Resolution not provided
3S8W D2 domain of human IFNAR2 Deposited 2011-05-31 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 131–232（102 aa） Fragment：UNP Residues 131-232
Non-standard monomer：Yes (specific site not provided by mmCIF) CL CHLORIDE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 8.5；293 K；31% (w/v) PEG 4000, 200 mM Li2SO4, 100 mM Tris pH 8.5, 5% (v/v) MPD, 10 mM Na acetate, 1.5% (w/v) PEG8000, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.60 Å R-free 0.270
3S8W D2 domain of human IFNAR2 Deposited 2011-05-31 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 131–232（102 aa） Fragment：UNP Residues 131-232
Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 8.5；293 K；31% (w/v) PEG 4000, 200 mM Li2SO4, 100 mM Tris pH 8.5, 5% (v/v) MPD, 10 mM Na acetate, 1.5% (w/v) PEG8000, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.60 Å R-free 0.270
3S8W D2 domain of human IFNAR2 Deposited 2011-05-31 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain C 131–232（102 aa） Fragment：UNP Residues 131-232
Non-standard monomer：Yes (specific site not provided by mmCIF) CL CHLORIDE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 8.5；293 K；31% (w/v) PEG 4000, 200 mM Li2SO4, 100 mM Tris pH 8.5, 5% (v/v) MPD, 10 mM Na acetate, 1.5% (w/v) PEG8000, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.60 Å R-free 0.270
3S9D binary complex between IFNa2 and IFNAR2 Deposited 2011-06-01 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 37–232（196 aa） Fragment：UNP Residues 37-232
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions 293 K；20% (w/v) PEG 3350, 200 mM NaSCN, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.00 Å R-free 0.233
3S9D binary complex between IFNa2 and IFNAR2 Deposited 2011-06-01 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain D 37–232（196 aa） Fragment：UNP Residues 37-232
Not recorded CL CHLORIDE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions 293 K；20% (w/v) PEG 3350, 200 mM NaSCN, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.00 Å R-free 0.233
3SE3 human IFNa2-IFNAR ternary complex Deposited 2011-06-10 Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain C 34–232（199 aa） Fragment：UNP Residues 34-232
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5；293 K；15% (w/v) PEG 3350, 100 mM Na malonate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 4.00 Å R-free 0.311

6 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name INAR2_HUMAN
Isoform —
PDB entities 3
Chains and sequence ranges Author chain C； PDBConstruct 1–199； UniProt 34–232

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 3se4

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3se4
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3se4
Deposition date deposition_date2011-06-10
Structure title titlehuman IFNw-IFNAR ternary complex
Keywords keywordsType I interferon signaling complex, extracellular space, IMMUNE SYSTEM RECEPTOR; IMMUNE SYSTEM RECEPTOR
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier31.33 Å
Radius of gyration Rg (electron density) rg_electron30.80 Å
Forward intensity I(0) i072860700.00
Molecular weight molecular_weight67752.0 kDa
Excluded volume excluded_volume84850 ų
Envelope volume envelope_volume112260 ų
Hydration-shell volume shell_volume32255 ų
Envelope diameter envelope_diameter114.9 Å
Shell Rg shell_rg35.65 Å
Envelope Rg envelope_rg30.89 Å
Shape Rg shape_rg30.80 Å
Total Rg total_rg31.25 Å
Total atoms total_atoms4784
Residues n_residues618
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax106.9 Å
Rg (real space) rg_real31.35 Å
Rg uncertainty (real space) rg_real_error0.81 Å
I(0) (real space) i0_real7.2860e+07
I(0) uncertainty (real space) i0_real_error1.1550e+06
Rg (reciprocal space) rg_reciprocal31.35 Å
I(0) (reciprocal space) i0_reciprocal72860000.0000
Solution quality estimate total_estimate0.8875
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary35.6 Å
Skewness Skewness skewness0.295
Kurtosis Kurtosis kurtosis-0.499
Angular range angular_range— – 0.2550 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha9587000.0000
Real-space data points n_real_points52
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.881; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.903; Smooth: 0.986
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

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7. Fold Classification (SCOP + CATH) 6 domains

CATH v4.4 (6 domains)

Domain ID domain_id3se4A01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id3se4A02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id3se4A03
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id3se4B00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1250 — Growth Hormone; Chain: A;
Homologous superfamily homologous superfamily10 —
Domain ID domain_id3se4C01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id3se4C02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
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8. Citations (1)

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9. Files and Curves (10)