3ezq

Crystal Structure of the Fas/FADD Death Domain Complex

Method: X-RAY DIFFRACTION D_max: 160.7 Å Quality: GOOD

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

Tumor necrosis factor receptor superfamily member 6

Homo sapiens

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 × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain A； UniProt 223–335 Chain C； UniProt 223–335	Fragment：Fas DD, UNP residues 223-335	Protein FADD × 2 （Q13158） SO4 SULFATE ION × 2 NA SODIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions：EVAPORATION；pH 4；291 K；0.95M citric acid, 1.9M ammonium sulfate, pH4, EVAPORATION, temperature 291K	Resolution 2.73 Å R-free 0.278
2	Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain E； UniProt 223–335 Chain G； UniProt 223–335	Fragment：Fas DD, UNP residues 223-335	Protein FADD × 2 （Q13158） SO4 SULFATE ION × 3 NA SODIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions：EVAPORATION；pH 4；291 K；0.95M citric acid, 1.9M ammonium sulfate, pH4, EVAPORATION, temperature 291K	Resolution 2.73 Å R-free 0.278
3	Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain I； UniProt 223–335 Chain K； UniProt 223–335	Fragment：Fas DD, UNP residues 223-335	Protein FADD × 2 （Q13158） SO4 SULFATE ION × 4 NA SODIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions：EVAPORATION；pH 4；291 K；0.95M citric acid, 1.9M ammonium sulfate, pH4, EVAPORATION, temperature 291K	Resolution 2.73 Å R-free 0.278
4	Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain M； UniProt 223–335 Chain O； UniProt 223–335	Fragment：Fas DD, UNP residues 223-335	Protein FADD × 2 （Q13158） SO4 SULFATE ION × 3 NA SODIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions：EVAPORATION；pH 4；291 K；0.95M citric acid, 1.9M ammonium sulfate, pH4, EVAPORATION, temperature 291K	Resolution 2.73 Å R-free 0.278

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.

Other PDB	Difference from Current Entry 3EZQ	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1DDF FAS DEATH DOMAIN, NMR, MINIMIZED AVERAGE STRUCTURE Deposited 1996-11-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 218–335（118 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 4	Resolution not provided
2NA7 Transmembrane domain of human Fas/CD95 death receptor Deposited 2015-12-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 171–198（28 aa） Fragment：Helical transmembrane residues 171-198 Chain B 171–198（28 aa） Fragment：Helical transmembrane residues 171-198 Chain C 171–198（28 aa） Fragment：Helical transmembrane residues 171-198	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.8；303 K；Ionic strength (raw mmCIF value) 50；Pressure ambient NMR sample composition 1 mM [U-100% 13C; U-100% 15N] Human Fas Transmembrane Domain, 60 mM [U-100% 2H] acyl chains DMPC, 120 mM [U-100% 2H] acyl chains DHPC, 20 mM sodium phosphate, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 1 mM [U-100% 13C; U-100% 15N; U-85% 2H] Human Fas Transmembrane Domain, 60 mM DMPC, 120 mM DHPC, 20 mM sodium phosphate, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 0.5 mM [U-100% 15N; U-100% 2H] Human Fas Transmembrane Domain, 0.5 mM [U-15% 13C] Human Fas Transmembrane Domain, 60 mM [U-100% 2H] acyl chains DMPC, 120 mM [U-100% 2H] acyl chains DHPC, 20 mM sodium phosphate, 95% H2O/5% D2O \| 95% H2O/5% D2O	Resolution not provided
3EWT Crystal Structure of calmodulin complexed with a peptide Deposited 2008-10-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain E 230–254（25 aa） Fragment：Helix(1+2) of death domain	Not recorded	CA CALCIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；pH 5.5；293 K；25%(w/v) PEG8000, 0.2M Sodium Acetate, 0.1M Sodium cacodylate, pH 5.5, EVAPORATION, temperature 293K	Resolution 2.40 Å R-free 0.259
3THM Crystal structure of Fas receptor extracellular domain in complex with Fab EP6b_B01 Deposited 2011-08-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 3 PDB declaration: trimeric	Chain F 17–172（156 aa） Fragment：extracellular domain	Not recorded	EDO 1,2-ETHANEDIOL × 5	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；277 K；20% PEG4000, 10% isopropanol, 100 mM HEPES/NaOH, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K	Resolution 2.10 Å R-free 0.221
3TJE Crystal structure of Fas receptor extracellular domain in complex with Fab E09 Deposited 2011-08-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain F 17–172（156 aa）	Not recorded	EDO 1,2-ETHANEDIOL × 5 CL CHLORIDE ION × 1 CD CADMIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；277 K；20% PEG4000, 5 mM CdCl2, 100 mM Tris/HOAc, pH 8.5, vapor diffusion, sitting drop, temperature 277K	Resolution 1.93 Å R-free 0.232
9NCQ Cryo-EM structure of Fas-FADD complex Deposited 2025-02-17	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: 12-meric	Chain A 225–320（96 aa） Chain B 225–320（96 aa） Chain C 225–320（96 aa） Chain D 225–320（96 aa） Chain E 225–320（96 aa） Chain F 225–320（96 aa） Chain G 225–320（96 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.51 Å

6 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	TNR6_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–113； UniProt 223–335 Author chain C； PDBConstruct 1–113； UniProt 223–335 Author chain E； PDBConstruct 1–113； UniProt 223–335 Author chain G； PDBConstruct 1–113； UniProt 223–335 Author chain I； PDBConstruct 1–113； UniProt 223–335 Author chain K； PDBConstruct 1–113； UniProt 223–335 Author chain M； PDBConstruct 1–113； UniProt 223–335 Author chain O； PDBConstruct 1–113； UniProt 223–335

Protein FADD

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 × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain B； UniProt 93–208 Chain D； UniProt 93–208	Fragment：Fadd DD, UNP residues 93-208	Tumor necrosis factor receptor superfamily member 6 × 2 （P25445） SO4 SULFATE ION × 2 NA SODIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions：EVAPORATION；pH 4；291 K；0.95M citric acid, 1.9M ammonium sulfate, pH4, EVAPORATION, temperature 291K	Resolution 2.73 Å R-free 0.278
2	Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain F； UniProt 93–208 Chain H； UniProt 93–208	Fragment：Fadd DD, UNP residues 93-208	Tumor necrosis factor receptor superfamily member 6 × 2 （P25445） SO4 SULFATE ION × 3 NA SODIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions：EVAPORATION；pH 4；291 K；0.95M citric acid, 1.9M ammonium sulfate, pH4, EVAPORATION, temperature 291K	Resolution 2.73 Å R-free 0.278
3	Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain J； UniProt 93–208 Chain L； UniProt 93–208	Fragment：Fadd DD, UNP residues 93-208	Tumor necrosis factor receptor superfamily member 6 × 2 （P25445） SO4 SULFATE ION × 4 NA SODIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions：EVAPORATION；pH 4；291 K；0.95M citric acid, 1.9M ammonium sulfate, pH4, EVAPORATION, temperature 291K	Resolution 2.73 Å R-free 0.278
4	Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain N； UniProt 93–208 Chain P； UniProt 93–208	Fragment：Fadd DD, UNP residues 93-208	Tumor necrosis factor receptor superfamily member 6 × 2 （P25445） SO4 SULFATE ION × 3 NA SODIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions：EVAPORATION；pH 4；291 K；0.95M citric acid, 1.9M ammonium sulfate, pH4, EVAPORATION, temperature 291K	Resolution 2.73 Å R-free 0.278

Other States of the Same Protein in the Database

Other PDB	Difference from Current Entry 3EZQ	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1A1W FADD DEATH EFFECTOR DOMAIN, F25Y MUTANT, NMR MINIMIZED AVERAGE STRUCTURE Deposited 1997-12-18	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–83（83 aa） Fragment：DEATH EFFECTOR DOMAIN	Mutation：F25Y	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 4；288 K	Resolution not provided
1A1Z FADD DEATH EFFECTOR DOMAIN, F25G MUTANT, NMR MINIMIZED AVERAGE STRUCTURE Deposited 1997-12-18	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–83（83 aa） Fragment：DEATH EFFECTOR DOMAIN	Mutation：F25G	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 4；288 K；Ionic strength (raw mmCIF value) 100 mM；Pressure 1 NMR sample composition H2O	Resolution not provided
1E3Y Death domain from human FADD/MORT1 Deposited 2000-06-26	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 93–192（100 aa） Fragment：DEATH DOMAIN RESIDUES 93-192	Mutation：YES	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.2；298 K；Ionic strength (raw mmCIF value) 50 MM PHOSPHATE BUFFER, 150MM NACL；Pressure 1	Resolution not provided
1E41 Death domain from human FADD/MORT1 Deposited 2000-06-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 93–192（100 aa） Fragment：DEATH DOMAIN RESIDUES 93-192	Mutation：YES	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.2；298 K；Ionic strength (raw mmCIF value) 50 MM PHOSPHATE BUFFER, 150MM NACL；Pressure 1	Resolution not provided
2GF5 Structure of intact FADD (MORT1) Deposited 2006-03-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–191（190 aa）	Mutation：F25Y	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7；288 K；Ionic strength (raw mmCIF value) 200mM phosphate；Pressure 1 NMR sample composition 200mM phosphate buffer, 95% H2O 5% D2O \| 95% H2O/5% D2O	Resolution not provided
3OQ9 Structure of the FAS/FADD death domain assembly Deposited 2010-09-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 10 PDB declaration: decameric	Chain H 93–184（92 aa） Fragment：UNP residues 93-184 Chain I 93–184（92 aa） Fragment：UNP residues 93-184 Chain J 93–184（92 aa） Fragment：UNP residues 93-184 Chain K 93–184（92 aa） Fragment：UNP residues 93-184 Chain L 93–184（92 aa） Fragment：UNP residues 93-184	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions hanging drop；pH 8.5；298 K；0.1 M Tris pH 8.5, 100 mM MgCl2, 5 % glycerol and 6-10 % PEG4000, hanging drop, temperature 298K	Resolution 6.80 Å R-free 0.354
6ACI Crystal structure of EPEC effector NleB in complex with FADD death domain Deposited 2018-07-26	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain H 93–184（92 aa）	Not recorded	UDP URIDINE-5'-DIPHOSPHATE × 1 MN MANGANESE (II) ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；4.5 M Sodium chloride, 100 mM HEPES pH 7.5	Resolution 1.87 Å R-free 0.209
8YBX Structure of the FADD/Caspase-8/cFLIP death effector domain assembly Deposited 2024-02-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 10 PDB declaration: decameric	Chain L 1–208（208 aa） Chain Q 1–208（208 aa） Chain R 1–208（208 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.68 Å
8YD7 Structure of FADD/Caspase-8/cFLIP death effector domain assembly Deposited 2024-02-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 10 PDB declaration: decameric	Chain L 1–208（208 aa）	Mutation：H9G Non-standard monomer：Yes (specific site not provided by mmCIF)	SE SELENIUM ATOM × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293.15 K；HEPES, TBG, PEG8000, TCEP, sodium chloride	Resolution 3.32 Å R-free 0.231
8YD8 Structure of FADD/Caspase-8/cFLIP death effector domain assembly Deposited 2024-02-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 10 PDB declaration: decameric	Chain L 1–208（208 aa）	Mutation：H9G	No recorded non-water small molecule	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
8YNI Structure of the FADD/Caspase-8/cFLIP death effector domain assembly Deposited 2024-03-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 11 PDB declaration: 11-meric	Chain L 1–208（208 aa） Chain Q 1–208（208 aa） Chain R 1–208（208 aa）	Mutation：F25G Mutation：F25G Mutation：F25G	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.66 Å
9L5W FADD-DED filaments coordinate complex IIa assembly during TNF-induced apoptosis Deposited 2024-12-23	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 18 PDB declaration: 18-meric	Chain A 1–91（91 aa） Chain B 1–91（91 aa） Chain C 1–91（91 aa） Chain D 1–91（91 aa） Chain E 1–91（91 aa） Chain F 1–91（91 aa） Chain G 1–91（91 aa） Chain H 1–91（91 aa） Chain I 1–91（91 aa） Chain J 1–91（91 aa） Chain K 1–91（91 aa） Chain L 1–91（91 aa） Chain M 1–91（91 aa） Chain N 1–91（91 aa） Chain O 1–91（91 aa） Chain P 1–91（91 aa） Chain Q 1–91（91 aa） Chain R 1–91（91 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4；25mM HEPES, 150mM NaCl cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.60 Å
9N94 Cryo-EM structure of FADD_DED filament Deposited 2025-02-10	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric	Chain A 1–208（208 aa） Chain B 1–208（208 aa） Chain C 1–208（208 aa） Chain D 1–208（208 aa） Chain E 1–208（208 aa） Chain F 1–208（208 aa） Chain G 1–208（208 aa） Chain H 1–208（208 aa） Chain I 1–208（208 aa） Chain J 1–208（208 aa） Chain K 1–208（208 aa） Chain L 1–208（208 aa） Chain M 1–208（208 aa） Chain N 1–208（208 aa） Chain O 1–208（208 aa） Chain P 1–208（208 aa） Chain Q 1–208（208 aa） Chain R 1–208（208 aa） Chain S 1–208（208 aa） Chain T 1–208（208 aa） Chain U 1–208（208 aa） Chain V 1–208（208 aa） Chain W 1–208（208 aa） Chain X 1–208（208 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.07 Å
9NCQ Cryo-EM structure of Fas-FADD complex Deposited 2025-02-17	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: 12-meric	Chain H 91–191（101 aa） Chain I 91–191（101 aa） Chain J 91–191（101 aa） Chain K 91–191（101 aa） Chain L 91–191（101 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.51 Å
9U6E FADD-DED filaments coordinate complex IIa assembly during TNF-induced apoptosis Deposited 2025-03-23	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric	Chain B 1–208（208 aa） Chain C 1–208（208 aa） Chain D 1–208（208 aa） Chain E 1–208（208 aa） Chain F 1–208（208 aa） Chain G 1–208（208 aa） Chain H 1–208（208 aa） Chain I 1–208（208 aa） Chain J 1–208（208 aa） Chain K 1–208（208 aa） Chain L 1–208（208 aa） Chain M 1–208（208 aa） Chain N 1–208（208 aa） Chain O 1–208（208 aa） Chain P 1–208（208 aa） Chain Q 1–208（208 aa） Chain R 1–208（208 aa） Chain S 1–208（208 aa） Chain T 1–208（208 aa） Chain U 1–208（208 aa） Chain V 1–208（208 aa） Chain W 1–208（208 aa） Chain X 1–208（208 aa） Chain Y 1–208（208 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5；25mM HEPES, 150mM NaCl cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.40 Å
9U7A FADD-DED filaments coordinate complex IIa assembly during TNF-induced apoptosis Deposited 2025-03-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric	Chain B 1–92（92 aa） Chain C 1–92（92 aa） Chain D 1–92（92 aa） Chain E 1–92（92 aa） Chain F 1–92（92 aa） Chain G 1–92（92 aa） Chain H 1–92（92 aa） Chain I 1–92（92 aa） Chain J 1–92（92 aa） Chain K 1–92（92 aa） Chain L 1–92（92 aa） Chain M 1–92（92 aa） Chain N 1–92（92 aa） Chain O 1–92（92 aa） Chain P 1–92（92 aa） Chain Q 1–92（92 aa） Chain R 1–92（92 aa） Chain S 1–92（92 aa） Chain T 1–92（92 aa） Chain U 1–92（92 aa） Chain V 1–92（92 aa） Chain W 1–92（92 aa） Chain X 1–92（92 aa） Chain Y 1–92（92 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5；25mM HEPES, 150mM NaCl cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.82 Å

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

View Construct and Data Evidence

UniProt name	FADD_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–116； UniProt 93–208 Author chain D； PDBConstruct 1–116； UniProt 93–208 Author chain F； PDBConstruct 1–116； UniProt 93–208 Author chain H； PDBConstruct 1–116； UniProt 93–208 Author chain J； PDBConstruct 1–116； UniProt 93–208 Author chain L； PDBConstruct 1–116； UniProt 93–208 Author chain N； PDBConstruct 1–116； UniProt 93–208 Author chain P； PDBConstruct 1–116； UniProt 93–208

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

P(r) Distance Distribution P(r) Distribution

Download Download SAXS (.dat) P(r) (.pr.out) CIF

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	3ezq
Deposition date deposition_date	2008-10-23
Structure title title	Crystal Structure of the Fas/FADD Death Domain Complex
Keywords keywords	Apoptosis, DISC, FAS, FADD, Membrane, receptor, Transmembrane; APOPTOSIS
Experimental Method method	X-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier	45.53 Å
Radius of gyration Rg (electron density) rg_electron	45.33 Å
Forward intensity I(0) i0	621498000.00
Molecular weight molecular_weight	196490.0 kDa
Excluded volume excluded_volume	243290 Å³
Envelope volume envelope_volume	356310 Å³
Hydration-shell volume shell_volume	67532 Å³
Envelope diameter envelope_diameter	169.9 Å
Shell Rg shell_rg	47.68 Å
Envelope Rg envelope_rg	44.71 Å
Shape Rg shape_rg	45.35 Å
Total Rg total_rg	45.37 Å
Total atoms total_atoms	13756
Residues n_residues	1712
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	160.7 Å
Rg (real space) rg_real	45.67 Å
Rg uncertainty (real space) rg_real_error	1.63 Å
I(0) (real space) i0_real	6.2150e+08
I(0) uncertainty (real space) i0_real_error	1.1690e+07
Rg (reciprocal space) rg_reciprocal	45.53 Å
I(0) (reciprocal space) i0_reciprocal	621400000.0000
Solution quality estimate total_estimate	0.8408
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	50.5 Å
Skewness Skewness skewness	0.490
Kurtosis Kurtosis kurtosis	-0.024
Angular range angular_range	— – 0.1750 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	40620000.0000
Real-space data points n_real_points	36
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.692; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.979; Smooth: 0.870

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Description description	Tumor necrosis factor receptor superfamily member 6
Molecular weight formula_weight	13061.8 kDa
Source method src_method	man
Copy count entity_count	8

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,C,E,G,I,K,M,O
Atom count atom_count	13933

NLSDVDLSKYITTIAGVMTLSQVKGFVRKNGVNEAKIDEIKNDNVQDTAEQKVQLLRNWHQLHGKKEAYDTLIKDLKKANLCTLAEKIQTIILKDITSDSENSNFRNEIQSLVLE

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	Human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	Protein FADD
Molecular weight formula_weight	13955.5 kDa
Source method src_method	man
Copy count entity_count	8

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B,D,F,H,J,L,N,P

GEEDLCAAFNVICDNVGKDWRRLARQLKVSDTKIDSIEDRYPRNLTERVRESLRIWKNTEKENATVAHLVGALRSCQMNLVADLVQEVQQARDLQNRSGAMSPMSWNSDASTSEASHHHHHH

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	Human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Escherichia coli

Entity 3 Entity 3 non-polymer

Description description	SULFATE ION
Molecular weight formula_weight	96.1 kDa
Source method src_method	syn
Copy count entity_count	12

Entity 4 Entity 4 non-polymer

Description description	SODIUM ION
Molecular weight formula_weight	23.0 kDa
Source method src_method	syn
Copy count entity_count	8

Entity 5 Entity 5 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	177

▼

7. Fold Classification (SCOP + CATH) 40 domains

SCOP 2.08 (24 domains)

Domain ID domain_id	d3ezqa1
Class class	a — All alpha proteins
Fold Fold fold	a.77 — DEATH domain
Superfamily Superfamily superfamily	a.77.1 — DEATH domain
Family Family family	a.77.1.2 — DEATH domain, DD

Domain ID domain_id	d3ezqa2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d3ezqb_
Class class	a — All alpha proteins
Fold Fold fold	a.77 — DEATH domain
Superfamily Superfamily superfamily	a.77.1 — DEATH domain
Family Family family	a.77.1.2 — DEATH domain, DD

Domain ID domain_id	d3ezqc1
Class class	a — All alpha proteins
Fold Fold fold	a.77 — DEATH domain
Superfamily Superfamily superfamily	a.77.1 — DEATH domain
Family Family family	a.77.1.2 — DEATH domain, DD

Domain ID domain_id	d3ezqc2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d3ezqd_
Class class	a — All alpha proteins
Fold Fold fold	a.77 — DEATH domain
Superfamily Superfamily superfamily	a.77.1 — DEATH domain
Family Family family	a.77.1.2 — DEATH domain, DD

Domain ID domain_id	d3ezqe1
Class class	a — All alpha proteins
Fold Fold fold	a.77 — DEATH domain
Superfamily Superfamily superfamily	a.77.1 — DEATH domain
Family Family family	a.77.1.2 — DEATH domain, DD

Domain ID domain_id	d3ezqe2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d3ezqf_
Class class	a — All alpha proteins
Fold Fold fold	a.77 — DEATH domain
Superfamily Superfamily superfamily	a.77.1 — DEATH domain
Family Family family	a.77.1.2 — DEATH domain, DD

Domain ID domain_id	d3ezqg1
Class class	a — All alpha proteins
Fold Fold fold	a.77 — DEATH domain
Superfamily Superfamily superfamily	a.77.1 — DEATH domain
Family Family family	a.77.1.2 — DEATH domain, DD

Domain ID domain_id	d3ezqg2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d3ezqh_
Class class	a — All alpha proteins
Fold Fold fold	a.77 — DEATH domain
Superfamily Superfamily superfamily	a.77.1 — DEATH domain
Family Family family	a.77.1.2 — DEATH domain, DD

Domain ID domain_id	d3ezqi1
Class class	a — All alpha proteins
Fold Fold fold	a.77 — DEATH domain
Superfamily Superfamily superfamily	a.77.1 — DEATH domain
Family Family family	a.77.1.2 — DEATH domain, DD

Domain ID domain_id	d3ezqi2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d3ezqj_
Class class	a — All alpha proteins
Fold Fold fold	a.77 — DEATH domain
Superfamily Superfamily superfamily	a.77.1 — DEATH domain
Family Family family	a.77.1.2 — DEATH domain, DD

Domain ID domain_id	d3ezqk1
Class class	a — All alpha proteins
Fold Fold fold	a.77 — DEATH domain
Superfamily Superfamily superfamily	a.77.1 — DEATH domain
Family Family family	a.77.1.2 — DEATH domain, DD

Domain ID domain_id	d3ezqk2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d3ezql_
Class class	a — All alpha proteins
Fold Fold fold	a.77 — DEATH domain
Superfamily Superfamily superfamily	a.77.1 — DEATH domain
Family Family family	a.77.1.2 — DEATH domain, DD

Domain ID domain_id	d3ezqm1
Class class	a — All alpha proteins
Fold Fold fold	a.77 — DEATH domain
Superfamily Superfamily superfamily	a.77.1 — DEATH domain
Family Family family	a.77.1.2 — DEATH domain, DD

Domain ID domain_id	d3ezqm2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d3ezqn_
Class class	a — All alpha proteins
Fold Fold fold	a.77 — DEATH domain
Superfamily Superfamily superfamily	a.77.1 — DEATH domain
Family Family family	a.77.1.2 — DEATH domain, DD

Domain ID domain_id	d3ezqo1
Class class	a — All alpha proteins
Fold Fold fold	a.77 — DEATH domain
Superfamily Superfamily superfamily	a.77.1 — DEATH domain
Family Family family	a.77.1.2 — DEATH domain, DD

Domain ID domain_id	d3ezqo2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d3ezqp_
Class class	a — All alpha proteins
Fold Fold fold	a.77 — DEATH domain
Superfamily Superfamily superfamily	a.77.1 — DEATH domain
Family Family family	a.77.1.2 — DEATH domain, DD

CATH v4.4 (16 domains)

Domain ID domain_id	3ezqA00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	533 — Death Domain, Fas
Homologous superfamily homologous superfamily	10 — Death Domain, Fas

Domain ID domain_id	3ezqB00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	533 — Death Domain, Fas
Homologous superfamily homologous superfamily	10 — Death Domain, Fas

Domain ID domain_id	3ezqC00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	533 — Death Domain, Fas
Homologous superfamily homologous superfamily	10 — Death Domain, Fas

Domain ID domain_id	3ezqD00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	533 — Death Domain, Fas
Homologous superfamily homologous superfamily	10 — Death Domain, Fas

Domain ID domain_id	3ezqE00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	533 — Death Domain, Fas
Homologous superfamily homologous superfamily	10 — Death Domain, Fas

Domain ID domain_id	3ezqF00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	533 — Death Domain, Fas
Homologous superfamily homologous superfamily	10 — Death Domain, Fas

Domain ID domain_id	3ezqG00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	533 — Death Domain, Fas
Homologous superfamily homologous superfamily	10 — Death Domain, Fas

Domain ID domain_id	3ezqH00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	533 — Death Domain, Fas
Homologous superfamily homologous superfamily	10 — Death Domain, Fas

Domain ID domain_id	3ezqI00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	533 — Death Domain, Fas
Homologous superfamily homologous superfamily	10 — Death Domain, Fas

Domain ID domain_id	3ezqJ00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	533 — Death Domain, Fas
Homologous superfamily homologous superfamily	10 — Death Domain, Fas

Domain ID domain_id	3ezqK00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	533 — Death Domain, Fas
Homologous superfamily homologous superfamily	10 — Death Domain, Fas

Domain ID domain_id	3ezqL00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	533 — Death Domain, Fas
Homologous superfamily homologous superfamily	10 — Death Domain, Fas

Domain ID domain_id	3ezqM00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	533 — Death Domain, Fas
Homologous superfamily homologous superfamily	10 — Death Domain, Fas

Domain ID domain_id	3ezqN00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	533 — Death Domain, Fas
Homologous superfamily homologous superfamily	10 — Death Domain, Fas

Domain ID domain_id	3ezqO00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	533 — Death Domain, Fas
Homologous superfamily homologous superfamily	10 — Death Domain, Fas

Domain ID domain_id	3ezqP00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	533 — Death Domain, Fas
Homologous superfamily homologous superfamily	10 — Death Domain, Fas

▶

8. Citations (1)

▶

Unit-cell length a length_a	126.218 Å
Unit-cell length b length_b	126.218 Å
Unit-cell length c length_c	299.274 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	120.00 °
Molecules per unit cell Z z_pdb	48

Space group space_group	P 61
Space-group number int_tables_number	169
Crystal system crystal_system	—

Resolution resolution	2.730 Å
Low-resolution limit resolution_low	30.000 Å
R factor r_factor	0.2361
R_work r_work	0.2339
R_free r_free	0.2780

Crystal Structure of the Fas/FADD Death Domain Complex

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

Tumor necrosis factor receptor superfamily member 6

State in the Current Structure

Other States of the Same Protein in the Database

Protein FADD

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

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

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 water

7. Fold Classification (SCOP + CATH) 40 domains

SCOP 2.08 (24 domains)

CATH v4.4 (16 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

fit	/app/data/saxs_computation/ez/3ezq/3ezq.fit
pddf	/app/data/pr_computation/ez/3ezq/3ezq.pr.out
profile	/app/data/saxs_computation/ez/3ezq/3ezq.dat