8ynn

Structure of the Caspase-8/cFLIP death effector domain assembly

Method: ELECTRON MICROSCOPY Dmax: 109.4 Å Quality: GOOD

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

Caspase-8 subunit p10

Homo sapiens

UniProt Q14790

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 × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain A; UniProt 1–479 Chain B; UniProt 1–479 Chain C; UniProt 1–479 Mutation:F122G, L123G, C360A, D374A, D384A CASP8 and FADD-like apoptosis regulator subunit p43 × 4 (O15519) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.97 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.

33 other PDB entries and 45 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CASP8_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–479; UniProt 1–479 Author chain B; PDBConstruct 1–479; UniProt 1–479 Author chain C; PDBConstruct 1–479; UniProt 1–479

CASP8 and FADD-like apoptosis regulator subunit p43

Homo sapiens

UniProt O15519

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 × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain H; UniProt 1–181 Chain I; UniProt 1–181 Chain J; UniProt 1–181 Chain K; UniProt 1–181 Not recorded Caspase-8 subunit p10 × 3 (Q14790) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.97 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.

15 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CFLAR_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain H; PDBConstruct 1–181; UniProt 1–181 Author chain I; PDBConstruct 1–181; UniProt 1–181 Author chain J; PDBConstruct 1–181; UniProt 1–181 Author chain K; PDBConstruct 1–181; UniProt 1–181

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 8ynn

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8ynn
Deposition date deposition_date2024-03-11
最后修订 last_revision2024-10-30
Structure title titleStructure of the Caspase-8/cFLIP death effector domain assembly
Keywords keywordsFADD, caspase-8, cellular FLICE-like inhibitory protein, Death effector domain, APOPTOSIS; APOPTOSIS
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier36.57
Radius of gyration Rg (electron density) rg_electron35.50
Forward intensity I(0) i0306037000.00
Molecular weight molecular_weight144380.0 kDa
Excluded volume excluded_volume182880 ų
Envelope volume envelope_volume264360 ų
Hydration-shell volume shell_volume60226 ų
Envelope diameter envelope_diameter117.5
Shell Rg shell_rg43.85
Envelope Rg envelope_rg34.28
Shape Rg shape_rg35.50
Total Rg total_rg36.12
Total atoms total_atoms10119
Residues n_residues1232
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 dmax109.4
Rg (real space) rg_real36.26
Rg uncertainty (real space) rg_real_error0.51
I(0) (real space) i0_real3.0600e+08
I(0) uncertainty (real space) i0_real_error4.6650e+06
Rg (reciprocal space) rg_reciprocal36.46
I(0) (reciprocal space) i0_reciprocal306100000.0000
Solution quality estimate total_estimate0.8951
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary50.9
Skewness Skewness skewness0.003
Kurtosis Kurtosis kurtosis-0.504
Angular range angular_range— – 0.2150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha67110000.0000
Real-space data points n_real_points44
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.917; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.968; Smooth: 0.912

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)