9od7

Structure of disulfide-stabilized IL-18 variant

Method: X-RAY DIFFRACTION Dmax: 53.7 Å Quality: GOOD

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

Interleukin-18

Homo sapiens

UniProt Q14116

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 37–193 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;273.15 K;0.1M MIB buffer (mixing sodium malonate, imidazole, and boric acid in the molar ratios 2:3:3), pH 4.0, 25% PEG 1500 Resolution 1.90 Å R-free 0.195

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.

19 other PDB entries and 36 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IL18_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–157; UniProt 37–193

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 9od7

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9od7
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9od7
Deposition date deposition_date2025-04-25
最后修订 last_revision2025-07-30
Structure title titleStructure of disulfide-stabilized IL-18 variant
Keywords keywordsprotein structure, CYTOKINE; CYTOKINE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier16.65
Radius of gyration Rg (electron density) rg_electron15.18
Forward intensity I(0) i06533740.00
Molecular weight molecular_weight18153.0 kDa
Excluded volume excluded_volume22592 ų
Envelope volume envelope_volume26143 ų
Hydration-shell volume shell_volume14428 ų
Envelope diameter envelope_diameter53.0
Shell Rg shell_rg21.19
Envelope Rg envelope_rg15.56
Shape Rg shape_rg15.16
Total Rg total_rg16.36
Total atoms total_atoms1273
Residues n_residues158
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 dmax53.7
Rg (real space) rg_real16.54
Rg uncertainty (real space) rg_real_error0.30
I(0) (real space) i0_real6.5340e+06
I(0) uncertainty (real space) i0_real_error7.4680e+04
Rg (reciprocal space) rg_reciprocal16.55
I(0) (reciprocal space) i0_reciprocal6534000.0000
Solution quality estimate total_estimate0.8066
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary53.0
Skewness Skewness skewness0.120
Kurtosis Kurtosis kurtosis-0.330
Angular range angular_range— – 0.4800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1213000.0000
Real-space data points n_real_points78
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.830; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.991; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)