5vb9

IL-17A in complex with peptide

Method: X-RAY DIFFRACTION Dmax: 126.8 Å Quality: REASONABLE

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 38–155 Fragment:UNP residues 38-155 Peptide inhibitor × 2 EDO 1,2-ETHANEDIOL × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;281 K;Protein at 7.1 mg/ml in 10mM Bis-Tris pH 6.5, 10% glycerol, 150mM NaCl with 2 mM of peptide, equilibrated against a reservoir containing 20% PEG 3350 and 200mM Lithium Chloride. Resolution 1.70 Å R-free 0.211
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 38–155 Fragment:UNP residues 38-155 Peptide inhibitor × 2 EDO 1,2-ETHANEDIOL × 2 CL CHLORIDE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;281 K;Protein at 7.1 mg/ml in 10mM Bis-Tris pH 6.5, 10% glycerol, 150mM NaCl with 2 mM of peptide, equilibrated against a reservoir containing 20% PEG 3350 and 200mM Lithium Chloride. Resolution 1.70 Å R-free 0.211

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 2–119; UniProt 38–155 Author chain B; PDBConstruct 2–119; UniProt 38–155

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 5vb9

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5vb9
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5vb9
Deposition date deposition_date2017-03-28
Structure title titleIL-17A in complex with peptide
Keywords keywordsIL17, inhibitor, IMMUNE SYSTEM - INHIBITOR complex; IMMUNE SYSTEM / INHIBITOR
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier32.40
Radius of gyration Rg (electron density) rg_electron33.11
Forward intensity I(0) i014518600.00
Molecular weight molecular_weight27890.0 kDa
Excluded volume excluded_volume34407 ų
Envelope volume envelope_volume51928 ų
Hydration-shell volume shell_volume16795 ų
Envelope diameter envelope_diameter124.5
Shell Rg shell_rg30.21
Envelope Rg envelope_rg33.49
Shape Rg shape_rg33.09
Total Rg total_rg32.83
Total atoms total_atoms1955
Residues n_residues239
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 dmax126.8
Rg (real space) rg_real33.41
Rg uncertainty (real space) rg_real_error2.10
I(0) (real space) i0_real1.4520e+07
I(0) uncertainty (real space) i0_real_error2.9270e+05
Rg (reciprocal space) rg_reciprocal32.98
I(0) (reciprocal space) i0_reciprocal14510000.0000
Solution quality estimate total_estimate0.6707
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary20.7
Skewness Skewness skewness0.724
Kurtosis Kurtosis kurtosis-0.138
Angular range angular_range— – 0.2450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha803600.0000
Real-space data points n_real_points50
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.265; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.044; Smooth: 0.876

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id5vb9A01
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology90 — Cystine Knot Cytokines, subunit B
Homologous superfamily homologous superfamily10 — Cystine-knot cytokines
Domain ID domain_id5vb9B01
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)