SAXSdb — 3s98

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

Interferon alpha/beta receptor 1

Homo sapiens

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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain A； UniProt 30–332	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

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 3S98	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
3SE3 human IFNa2-IFNAR ternary complex Deposited 2011-06-10	Different construct Different mutation/modification Different oligomeric state 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
3SE4 human IFNw-IFNAR ternary complex Deposited 2011-06-10	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 28–436（409 aa） Fragment：IFNw (UNP Residues 28-436)	Mutation：N101Q	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
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 oligomeric state 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 oligomeric state 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	IFNAR1_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 4–306； UniProt 30–332

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	3s98
Deposition date deposition_date	2011-06-01
Structure title title	human IFNAR1
Keywords keywords	;human, type I interferons, receptor chain, IFNAR1, fibronectin type III, type I interferon receptor chain, extracellular space, SIGNALING PROTEIN RECEPTOR ;; SIGNALING PROTEIN RECEPTOR
Experimental Method method	X-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier	27.30 Å
Radius of gyration Rg (electron density) rg_electron	26.85 Å
Forward intensity I(0) i0	15833800.00
Molecular weight molecular_weight	30780.0 kDa
Excluded volume excluded_volume	38635 Å³
Envelope volume envelope_volume	49257 Å³
Hydration-shell volume shell_volume	17679 Å³
Envelope diameter envelope_diameter	94.0 Å
Shell Rg shell_rg	30.31 Å
Envelope Rg envelope_rg	26.67 Å
Shape Rg shape_rg	26.82 Å
Total Rg total_rg	27.41 Å
Total atoms total_atoms	2166
Residues n_residues	267
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	88.6 Å
Rg (real space) rg_real	28.32 Å
Rg uncertainty (real space) rg_real_error	0.30 Å
I(0) (real space) i0_real	1.5740e+07
I(0) uncertainty (real space) i0_real_error	1.9770e+05
Rg (reciprocal space) rg_reciprocal	27.57 Å
I(0) (reciprocal space) i0_reciprocal	15830000.0000
Solution quality estimate total_estimate	0.6008
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	19.9 Å
Skewness Skewness skewness	0.495
Kurtosis Kurtosis kurtosis	-0.599
Angular range angular_range	— – 0.2900 Å⁻¹
Current regularization parameter α current_alpha	6.5660
Highest regularization parameter α highest_alpha	2625000.0000
Real-space data points n_real_points	59
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.807; Stabil: 0.934; Sysdev: 0.000; Positv: 1.000; Valcen: 0.521; Smooth: 0.072

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	Interferon alpha/beta receptor 1
Molecular weight formula_weight	35641.8 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	2349

ADPLKSPQKVEVDIIDDNFILRWNRSDESVGNVTFSFDYQKTGMDNWIKLSGCQNITSTKCNFSSLKLNVYEEIKLRIRAEKENTSSWYEVDSFTPFRKAQIGPPEVHLEAEDKAIVIHISPGTKDSVMWALDGLSFTYSLVIWKNSSGVEERIENIYSRHKIYKLSPETTYCLKVKAALLTSWKIGVYSPVHCIKTTVENELPPPENIEVSVQNQNYVLKWDYTYANMTFQVQWLHAFLKRNPGNHLYKWKQIPDCENVKTTQCVFPQNVFQKGIYLLRVQASDGNNTSFWSEEIKFDTEIQAFL

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Trichoplusia ni

Entity 2 Entity 2 non-polymer

Description description	2-acetamido-2-deoxy-beta-D-glucopyranose
Molecular weight formula_weight	221.2 kDa
Source method src_method	man
Copy count entity_count	1

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	145

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7. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

Domain ID domain_id	3s98A01
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

Domain ID domain_id	3s98A02
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

Domain ID domain_id	3s98A03
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

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8. Citations (1)

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Unit-cell length a length_a	47.090 Å
Unit-cell length b length_b	86.180 Å
Unit-cell length c length_c	91.340 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	4

Space group space_group	P 21 21 21
Space-group number int_tables_number	19
Crystal system crystal_system	—

Resolution resolution	1.900 Å
Low-resolution limit resolution_low	19.486 Å
R factor r_factor	—
R_work r_work	0.2100
R_free r_free	0.2340

fit	/app/data/saxs_computation/s9/3s98/3s98.fit
pddf	/app/data/pr_computation/s9/3s98/3s98.pr.out
profile	/app/data/saxs_computation/s9/3s98/3s98.dat

human IFNAR1

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

Interferon alpha/beta receptor 1

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

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

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction