8spb

Caspase-4/Pro-IL-18 complex

Method: ELECTRON MICROSCOPY Dmax: 122.0 Å Quality: GOOD

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

Caspase-4 subunit p20

Homo sapiens

UniProt P49662

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 94–270 Chain B; UniProt 290–377 Chain a; UniProt 94–270 Chain b; UniProt 290–377 Not recorded Interleukin-18 × 2 (Q14116) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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.

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

View Construct and Data Evidence
UniProt name CASP4_HUMAN
Isoform
PDB entities 1, 2
Chains and sequence ranges Author chain A; PDBConstruct 31–207; UniProt 94–270 Author chain a; PDBConstruct 31–207; UniProt 94–270 Author chain B; PDBConstruct 5–92; UniProt 290–377 Author chain b; PDBConstruct 5–92; UniProt 290–377

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 heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain C; UniProt 6–193 Chain c; UniProt 6–193 Not recorded Caspase-4 subunit p20 × 2 (P49662) Caspase-4 subunit p10 × 2 (P49662) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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.

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 3
Chains and sequence ranges Author chain C; PDBConstruct 1–188; UniProt 6–193 Author chain c; PDBConstruct 1–188; UniProt 6–193

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 8spb

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8spb
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8spb
Deposition date deposition_date2023-05-02
Structure title titleCaspase-4/Pro-IL-18 complex
Keywords keywordsInnate immune, Complex, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier33.78
Radius of gyration Rg (electron density) rg_electron33.74
Forward intensity I(0) i0144311000.00
Molecular weight molecular_weight95848.0 kDa
Excluded volume excluded_volume119880 ų
Envelope volume envelope_volume160380 ų
Hydration-shell volume shell_volume41466 ų
Envelope diameter envelope_diameter129.9
Shell Rg shell_rg38.06
Envelope Rg envelope_rg34.66
Shape Rg shape_rg33.70
Total Rg total_rg34.20
Total atoms total_atoms6726
Residues n_residues828
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 dmax122.0
Rg (real space) rg_real34.02
Rg uncertainty (real space) rg_real_error1.38
I(0) (real space) i0_real1.4430e+08
I(0) uncertainty (real space) i0_real_error2.4250e+06
Rg (reciprocal space) rg_reciprocal33.87
I(0) (reciprocal space) i0_reciprocal144300000.0000
Solution quality estimate total_estimate0.8074
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary36.4
Skewness Skewness skewness0.646
Kurtosis Kurtosis kurtosis0.308
Angular range angular_range— – 0.2350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha46080000.0000
Real-space data points n_real_points48
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.672; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.774; Smooth: 0.703

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)