← Back to search
9ot1

Helical assembly of the IL-17RA/RB/ACT1 complex

Method: ELECTRON MICROSCOPY Dmax: 242.8 Å Quality: GOOD
▼

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

Interleukin-17 receptor B,Interleukin-17 receptor A

Homo sapiens

UniProt Q96F46

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 19 PDB declaration: 19-meric（19） Consistent with protein copy count Chain A； UniProt 361–866 Chain B； UniProt 361–866 Chain C； UniProt 361–866 Chain D； UniProt 361–866 Not recorded E3 ubiquitin ligase TRAF3IP2 × 15 （O43734） ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5 cryo-EM vitrification conditions：Cryogen NITROGEN Resolution 3.00 Å

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 9OT1 Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
3JVF Crystal structure of an Interleukin-17 receptor complex Deposited 2009-09-16 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Heteromer；Protein × 3 PDB declaration: trimeric
Chain C 32–317（286 aa） Fragment：extracellular domain
Non-standard monomer：Yes (specific site not provided by mmCIF) CA CALCIUM ION × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9.2；295 K；PEG6000, 0.1M CAPSO, calcium chloride, pH 9.2, VAPOR DIFFUSION, HANGING DROP, temperature 295K
Resolution 3.30 Å R-free 0.256
4HSA Structure of interleukin 17a in complex with il17ra receptor Deposited 2012-10-29 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Heteromer；Protein × 3 PDB declaration: trimeric
Chain C 32–317（286 aa）
Mutation：N175D, N234D No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 3.15 Å R-free 0.232
4HSA Structure of interleukin 17a in complex with il17ra receptor Deposited 2012-10-29 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Other combination Heteromer；Protein × 3 PDB declaration: trimeric
Chain F 32–317（286 aa）
Mutation：N175D, N234D NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 3.15 Å R-free 0.232
4NUX Structure of receptor A Deposited 2013-12-04 Different construct Different mutation/modification 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 376–591（216 aa） Fragment：SEFIR domain (UNP residues 376-591)
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION；pH 6；293 K；0.1M MES, 5%PEG6000, pH 6.0, EVAPORATION, temperature 293K
Resolution 2.29 Å R-free 0.242
5N9B Crystal Structure of unliganded human IL-17RA Deposited 2017-02-24 Different construct Different mutation/modification 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 33–318（286 aa） Fragment：Extracellular domain, UNP rsidues 33-318
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 7；293 K；Tris-HCl, PEG 2000 MME, lithium sulfate
Resolution 1.90 Å R-free 0.234
5NAN Crystal Structure of human IL-17AF in complex with human IL-17RA Deposited 2017-02-28 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Heteromer；Protein × 3 PDB declaration: trimeric
Chain B 33–320（288 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 7.5；293 K；0.1M HEPES, 15% PEG MME 5,000, 0.05M Ammonium Acetate
Resolution 3.30 Å R-free 0.243
5NAN Crystal Structure of human IL-17AF in complex with human IL-17RA Deposited 2017-02-28 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain C 33–320（288 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 7.5；293 K；0.1M HEPES, 15% PEG MME 5,000, 0.05M Ammonium Acetate
Resolution 3.30 Å R-free 0.243
7UWL Structure of the IL-25-IL-17RB-IL-17RA ternary complex Deposited 2022-05-03 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Heteromer；Protein × 6 PDB declaration: hexameric
Chain E 33–317（285 aa）
Chain F 33–317（285 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 14 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.70 Å
7UWM Structure of the IL-17A-IL-17RA binary complex Deposited 2022-05-03 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Heteromer；Protein × 6 PDB declaration: hexameric
Chain C 33–304（272 aa）
Chain F 33–304（272 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 7 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.50 Å
7UWN Structure of the IL-17A-IL-17RA-IL-17RC ternary complex Deposited 2022-05-03 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Heteromer；Protein × 7 PDB declaration: heptameric
Chain C 33–317（285 aa）
Chain F 33–317（285 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 9 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.01 Å
7ZAN Crystal Structure of human IL-17A in complex with IL-17RA and IL-17RC Deposited 2022-03-22 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric
Chain C 33–320（288 aa）
Mutation：N49D, N206D, N265D NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 8 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；0.1M MES, 10.0% PEG DME 500
Resolution 5.06 Å R-free 0.353

9 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name I17RA_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 178–683； UniProt 361–866 Author chain B； PDBConstruct 178–683； UniProt 361–866 Author chain C； PDBConstruct 178–683； UniProt 361–866 Author chain D； PDBConstruct 178–683； UniProt 361–866

Interleukin-17 receptor B,Interleukin-17 receptor A

Homo sapiens

UniProt Q9NRM6

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 19 PDB declaration: 19-meric（19） Consistent with protein copy count Chain A； UniProt 328–483 Chain B； UniProt 328–483 Chain C； UniProt 328–483 Chain D； UniProt 328–483 Not recorded E3 ubiquitin ligase TRAF3IP2 × 15 （O43734） ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5 cryo-EM vitrification conditions：Cryogen NITROGEN Resolution 3.00 Å

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 9OT1 Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
7UWJ Structure of the homodimeric IL-25-IL-17RB binary complex Deposited 2022-05-03 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain C 18–272（255 aa）
Chain D 18–272（255 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.20 Å
7UWK Structure of the higher-order IL-25-IL-17RB complex Deposited 2022-05-03 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain C 18–288（271 aa）
Chain D 18–288（271 aa）
Chain I 18–288（271 aa）
Chain J 18–288（271 aa）
Chain K 18–288（271 aa）
Chain L 18–288（271 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.40 Å
7UWL Structure of the IL-25-IL-17RB-IL-17RA ternary complex Deposited 2022-05-03 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Heteromer；Protein × 6 PDB declaration: hexameric
Chain C 18–288（271 aa）
Chain D 18–288（271 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 14 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.70 Å

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name I17RB_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 5–160； UniProt 328–483 Author chain B； PDBConstruct 5–160； UniProt 328–483 Author chain C； PDBConstruct 5–160； UniProt 328–483 Author chain D； PDBConstruct 5–160； UniProt 328–483

E3 ubiquitin ligase TRAF3IP2

Homo sapiens

UniProt O43734

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 19 PDB declaration: 19-meric（19） Consistent with protein copy count Chain E； UniProt 372–574 Chain F； UniProt 372–574 Chain G； UniProt 372–574 Chain H； UniProt 372–574 Chain I； UniProt 372–574 Chain J； UniProt 372–574 Chain K； UniProt 372–574 Chain L； UniProt 372–574 Chain M； UniProt 372–574 Chain N； UniProt 372–574 Chain O； UniProt 372–574 Chain P； UniProt 372–574 Chain Q； UniProt 372–574 Chain R； UniProt 372–574 Chain S； UniProt 372–574 Not recorded Interleukin-17 receptor B,Interleukin-17 receptor A × 4 （Q9NRM6,Q96F46） ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5 cryo-EM vitrification conditions：Cryogen NITROGEN Resolution 3.00 Å

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 CIKS_HUMAN
Isoform —
PDB entities 2
Chains and sequence ranges Author chain E； PDBConstruct 5–207； UniProt 372–574 Author chain F； PDBConstruct 5–207； UniProt 372–574 Author chain G； PDBConstruct 5–207； UniProt 372–574 Author chain H； PDBConstruct 5–207； UniProt 372–574 Author chain I； PDBConstruct 5–207； UniProt 372–574 Author chain J； PDBConstruct 5–207； UniProt 372–574 Author chain K； PDBConstruct 5–207； UniProt 372–574 Author chain L； PDBConstruct 5–207； UniProt 372–574 Author chain M； PDBConstruct 5–207； UniProt 372–574 Author chain N； PDBConstruct 5–207； UniProt 372–574 Author chain O； PDBConstruct 5–207； UniProt 372–574 Author chain P； PDBConstruct 5–207； UniProt 372–574 Author chain Q； PDBConstruct 5–207； UniProt 372–574 Author chain R； PDBConstruct 5–207； UniProt 372–574 Author chain S； PDBConstruct 5–207； UniProt 372–574

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 9ot1

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9ot1
Download Download
▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id9ot1
Deposition date deposition_date2025-05-26
Structure title titleHelical assembly of the IL-17RA/RB/ACT1 complex
Keywords keywordsIL-17 receptor, ACT1, helical assembly, IL-17, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodELECTRON MICROSCOPY
▼

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

Radius of gyration Rg (Guinier) rg_guinier89.07 Å
Radius of gyration Rg (electron density) rg_electron92.06 Å
Forward intensity I(0) i02105850000.00
Molecular weight molecular_weight407490.0 kDa
Excluded volume excluded_volume518430 ų
Envelope volume envelope_volume757320 ų
Hydration-shell volume shell_volume84227 ų
Envelope diameter envelope_diameter335.9 Å
Shell Rg shell_rg56.57 Å
Envelope Rg envelope_rg93.93 Å
Shape Rg shape_rg92.03 Å
Total Rg total_rg91.56 Å
Total atoms total_atoms57949
Residues n_residues3510
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
▼

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

Maximum dimension Dmax dmax242.8 Å
Rg (real space) rg_real81.72 Å
Rg uncertainty (real space) rg_real_error1.34 Å
I(0) (real space) i0_real2.0100e+09
I(0) uncertainty (real space) i0_real_error3.5740e+07
Rg (reciprocal space) rg_reciprocal80.24 Å
I(0) (reciprocal space) i0_reciprocal2052000000.0000
Solution quality estimate total_estimate0.8402
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary57.1 Å
Skewness Skewness skewness0.447
Kurtosis Kurtosis kurtosis-0.827
Angular range angular_range— – 0.0850 Å−1
Current regularization parameter α current_alpha0.4846
Highest regularization parameter α highest_alpha32470000.0000
Real-space data points n_real_points18
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.003; Oscil: 0.741; Stabil: 0.982; Sysdev: 1.000; Positv: 1.000; Valcen: 0.798; Smooth: 0.001
▶

5. Crystallography and Experiment 5. Crystallography & Experiment

▶

6. Entities and Polymers Entities & Polymers (3)

▶

8. Citations (1)

▶

9. Files and Curves (10)