8ybx

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

Method: ELECTRON MICROSCOPY
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Caspase-8 subunit p10

Homo sapiens

UniProt Q14790

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 10 CASP8 and FADD-like apoptosis regulator subunit p43 × 4 (O15519) FAS-associated death domain protein × 3 (Q13158) Consistent with protein count

Other States of the Same Protein in the Database

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 Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 10 Caspase-8 subunit p10 × 3 (Q14790) FAS-associated death domain protein × 3 (Q13158) Consistent with protein count

Other States of the Same Protein in the Database

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

FAS-associated death domain protein

Homo sapiens

UniProt Q13158

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 10 Caspase-8 subunit p10 × 3 (Q14790) CASP8 and FADD-like apoptosis regulator subunit p43 × 4 (O15519) Consistent with protein count

Other States of the Same Protein in the Database

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 Author chain Q; PDBConstruct 1–208; UniProt 1–208 Author chain R; 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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id8ybx
Deposition date deposition_date2024-02-16
Last revision last_revision2024-05-15
Structure title titleStructure of the FADD/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
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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

8ybx__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

8ybx__assembly_1__model_1 | I(q)

10-2 10-1 106 107 108 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

8ybx__assembly_1__model_1 | P(r) · Pending

The new assembly/model P(r) has not been calculated yet This placeholder does not display legacy data r (Angstrom) P(r)
P(r) will be calculated and displayed separately for the same assembly/model.
Rg(Guinier)38.68 Å
Rg (electron density)37.67 Å
Total Rg38.16 Å
Atom count12126
Residues1482
Excluded volume218760 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 8ybx__assembly_1__model_1 decameric (10) Success 4.1.3-1-20251215 (887e7ef) View Download
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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (3)

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7. Citations (1)