8yd8

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

Method: X-RAY DIFFRACTION Dmax: 127.0 Å Quality: REASONABLE

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

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 × 10 PDB declaration: decameric(10) 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 Mutation:H7G Caspase-8 × 5 (Q14790) FAS-associated death domain protein × 1 (Q13158) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293.15 K;HEPES, PEG 8000, TBG, TCEP, sodium chloride Resolution 3.11 Å R-free 0.241

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 1
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

Caspase-8

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain A; UniProt 1–185 Chain B; UniProt 1–185 Chain C; UniProt 1–185 Chain D; UniProt 1–185 Chain E; UniProt 1–185 Mutation:F122G, L123G CASP8 and FADD-like apoptosis regulator subunit p43 × 4 (O15519) FAS-associated death domain protein × 1 (Q13158) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293.15 K;HEPES, PEG 8000, TBG, TCEP, sodium chloride Resolution 3.11 Å R-free 0.241

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 2
Chains and sequence ranges Author chain A; PDBConstruct 1–185; UniProt 1–185 Author chain B; PDBConstruct 1–185; UniProt 1–185 Author chain C; PDBConstruct 1–185; UniProt 1–185 Author chain D; PDBConstruct 1–185; UniProt 1–185 Author chain E; PDBConstruct 1–185; UniProt 1–185

FAS-associated death domain protein

Homo sapiens

UniProt Q13158

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain L; UniProt 1–208 Mutation:H9G CASP8 and FADD-like apoptosis regulator subunit p43 × 4 (O15519) Caspase-8 × 5 (Q14790) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293.15 K;HEPES, PEG 8000, TBG, TCEP, sodium chloride Resolution 3.11 Å R-free 0.241

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.

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

View Construct and Data Evidence
UniProt name FADD_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain L; PDBConstruct 1–208; UniProt 1–208

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 8yd8

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8yd8
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8yd8
Deposition date deposition_date2024-02-19
最后修订 last_revision2024-05-15
Structure title titleStructure of FADD/Caspase-8/cFLIP death effector domain assembly
Keywords keywordsFADD, Caspase-8, cFLIP, death effector domain, APOPTOSIS; APOPTOSIS
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier39.95
Radius of gyration Rg (electron density) rg_electron39.16
Forward intensity I(0) i0552492000.00
Molecular weight molecular_weight196230.0 kDa
Excluded volume excluded_volume248250 ų
Envelope volume envelope_volume344580 ų
Hydration-shell volume shell_volume71660 ų
Envelope diameter envelope_diameter138.9
Shell Rg shell_rg46.49
Envelope Rg envelope_rg38.26
Shape Rg shape_rg39.17
Total Rg total_rg39.56
Total atoms total_atoms13754
Residues n_residues1676
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 dmax127.0
Rg (real space) rg_real39.74
Rg uncertainty (real space) rg_real_error0.82
I(0) (real space) i0_real5.5250e+08
I(0) uncertainty (real space) i0_real_error8.2140e+06
Rg (reciprocal space) rg_reciprocal39.87
I(0) (reciprocal space) i0_reciprocal552600000.0000
Solution quality estimate total_estimate0.6429
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary50.8
Skewness Skewness skewness0.249
Kurtosis Kurtosis kurtosis-0.209
Angular range angular_range— – 0.2000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha122200000.0000
Real-space data points n_real_points41
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.841; Stabil: 1.000; Sysdev: 0.013; Positv: 1.000; Valcen: 0.982; Smooth: 0.809

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)