5nan

Crystal Structure of human IL-17AF in complex with human IL-17RA

Method: X-RAY DIFFRACTION Dmax: 130.5 Å Quality: GOOD

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

Interleukin-17A

Homo sapiens

UniProt Q16552

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 × 3 其他Polymer 1 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 24–155 Not recorded Interleukin-17 receptor A × 1 (Q96F46) Interleukin-17F × 1 (Q96PD4) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[beta-D-galactopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose × 1 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
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain D; UniProt 24–155 Not recorded Interleukin-17 receptor A × 1 (Q96F46) Interleukin-17F × 1 (Q96PD4) 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

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.

43 other PDB entries and 55 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IL17_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–132; UniProt 24–155 Author chain D; PDBConstruct 1–132; UniProt 24–155

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 Other combination Heteromer Protein × 3 其他Polymer 1 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 33–320 Not recorded Interleukin-17A × 1 (Q16552) Interleukin-17F × 1 (Q96PD4) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[beta-D-galactopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose × 1 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
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 33–320 Not recorded Interleukin-17A × 1 (Q16552) Interleukin-17F × 1 (Q96PD4) 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

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.

9 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name I17RA_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–288; UniProt 33–320 Author chain C; PDBConstruct 1–288; UniProt 33–320

Interleukin-17F

Homo sapiens

UniProt Q96PD4

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 × 3 其他Polymer 1 PDB declaration: trimeric(3) Consistent with protein copy count Chain F; UniProt 31–163 Not recorded Interleukin-17A × 1 (Q16552) Interleukin-17 receptor A × 1 (Q96F46) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[beta-D-galactopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose × 1 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
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain E; UniProt 31–163 Not recorded Interleukin-17A × 1 (Q16552) Interleukin-17 receptor A × 1 (Q96F46) 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

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.

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

View Construct and Data Evidence
UniProt name IL17F_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain E; PDBConstruct 7–139; UniProt 31–163 Author chain F; PDBConstruct 7–139; UniProt 31–163

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 5nan

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5nan
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5nan
Deposition date deposition_date2017-02-28
Structure title titleCrystal Structure of human IL-17AF in complex with human IL-17RA
Keywords keywordsCystine-knot, Fibronectin type III, cytokine; CYTOKINE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier40.45
Radius of gyration Rg (electron density) rg_electron40.01
Forward intensity I(0) i0209233000.00
Molecular weight molecular_weight112960.0 kDa
Excluded volume excluded_volume139400 ų
Envelope volume envelope_volume200720 ų
Hydration-shell volume shell_volume41821 ų
Envelope diameter envelope_diameter131.1
Shell Rg shell_rg45.89
Envelope Rg envelope_rg38.97
Shape Rg shape_rg39.99
Total Rg total_rg40.41
Total atoms total_atoms7923
Residues n_residues972
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 dmax130.5
Rg (real space) rg_real40.50
Rg uncertainty (real space) rg_real_error1.09
I(0) (real space) i0_real2.0920e+08
I(0) uncertainty (real space) i0_real_error3.7460e+06
Rg (reciprocal space) rg_reciprocal40.45
I(0) (reciprocal space) i0_reciprocal209200000.0000
Solution quality estimate total_estimate0.8739
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary33.5
Skewness Skewness skewness0.197
Kurtosis Kurtosis kurtosis-0.859
Angular range angular_range— – 0.1950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha16880000.0000
Real-space data points n_real_points40
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.874; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.856; Smooth: 0.878

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 8 domains

CATH v4.4 (8 domains)

Domain ID domain_id5nanA01
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology90 — Cystine Knot Cytokines, subunit B
Homologous superfamily homologous superfamily10 — Cystine-knot cytokines
Domain ID domain_id5nanB01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily2160 — Interleukin-17 receptor A/B, fibronectin-III-like domain 1
Domain ID domain_id5nanB02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily2150 — Interleukin-17 receptor A/B, fibronectin-III-like domain 2
Domain ID domain_id5nanC01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily2160 — Interleukin-17 receptor A/B, fibronectin-III-like domain 1
Domain ID domain_id5nanC02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily2150 — Interleukin-17 receptor A/B, fibronectin-III-like domain 2
Domain ID domain_id5nanD01
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology90 — Cystine Knot Cytokines, subunit B
Homologous superfamily homologous superfamily10 — Cystine-knot cytokines
Domain ID domain_id5nanE00
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology90 — Cystine Knot Cytokines, subunit B
Homologous superfamily homologous superfamily10 — Cystine-knot cytokines
Domain ID domain_id5nanF00
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology90 — Cystine Knot Cytokines, subunit B
Homologous superfamily homologous superfamily10 — Cystine-knot cytokines

8. Citations (1)

9. Files and Curves (10)