7zan

Crystal Structure of human IL-17A in complex with IL-17RA and IL-17RC

Method: X-RAY DIFFRACTION Dmax: 142.1 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 Protein heterocomplex Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 34–155 Chain B; UniProt 34–155 Fragment:IL-17A Mutation:N68D,C129S Interleukin-17 receptor A × 2 (Q96F46) Isoform 2 of Interleukin-17 receptor C × 2 (Q8NAC3) 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

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 56 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 2–123; UniProt 34–155 Author chain B; PDBConstruct 2–123; UniProt 34–155

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 Protein heterocomplex Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain C; UniProt 33–320 Mutation:N49D, N206D, N265D Interleukin-17A × 4 (Q16552) Isoform 2 of Interleukin-17 receptor C × 2 (Q8NAC3) 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

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 11 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 C; PDBConstruct 1–288; UniProt 33–320

Isoform 2 of Interleukin-17 receptor C

Homo sapiens

UniProt Q8NAC3

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain D; UniProt 21–467 Fragment:Extracellular domain Interleukin-17A × 4 (Q16552) Interleukin-17 receptor A × 2 (Q96F46) 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

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.

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

View Construct and Data Evidence
UniProt name I17RC_HUMAN
Isoform Q8NAC3-2
PDB entities 3
Chains and sequence ranges Author chain D; PDBConstruct 1–447; UniProt 21–467

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 7zan

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7zan
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7zan
Deposition date deposition_date2022-03-22
Structure title titleCrystal Structure of human IL-17A in complex with IL-17RA and IL-17RC
Keywords keywordsImmune system, CYTOKINE; CYTOKINE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier39.46
Radius of gyration Rg (electron density) rg_electron40.04
Forward intensity I(0) i0182225000.00
Molecular weight molecular_weight105540.0 kDa
Excluded volume excluded_volume130800 ų
Envelope volume envelope_volume188620 ų
Hydration-shell volume shell_volume42680 ų
Envelope diameter envelope_diameter148.9
Shell Rg shell_rg41.24
Envelope Rg envelope_rg40.39
Shape Rg shape_rg40.03
Total Rg total_rg40.17
Total atoms total_atoms14519
Residues n_residues921
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 dmax142.1
Rg (real space) rg_real39.99
Rg uncertainty (real space) rg_real_error1.49
I(0) (real space) i0_real1.8220e+08
I(0) uncertainty (real space) i0_real_error3.7650e+06
Rg (reciprocal space) rg_reciprocal39.66
I(0) (reciprocal space) i0_reciprocal182200000.0000
Solution quality estimate total_estimate0.8092
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary39.1
Skewness Skewness skewness0.627
Kurtosis Kurtosis kurtosis0.018
Angular range angular_range— – 0.2000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha24640000.0000
Real-space data points n_real_points41
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.707; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.738; Smooth: 0.658

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)