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1a1w

FADD DEATH EFFECTOR DOMAIN, F25Y MUTANT, NMR MINIMIZED AVERAGE STRUCTURE

Method: SOLUTION NMR Dmax: 44.6 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

FADD 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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain A； UniProt 1–83 Fragment：DEATH EFFECTOR DOMAIN Mutation：F25Y No other associated polymer SOLUTION NMR NMR measurement conditions：pH 4；288 K Resolution not provided

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 1A1W Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1A1Z FADD DEATH EFFECTOR DOMAIN, F25G MUTANT, NMR MINIMIZED AVERAGE STRUCTURE Deposited 1997-12-18 Different mutation/modification Different experimental conditions 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 experimental conditions 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 experimental conditions 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 experimental conditions 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
3EZQ Crystal Structure of the Fas/FADD Death Domain Complex Deposited 2008-10-23 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 93–208（116 aa） Fragment：Fadd DD, UNP residues 93-208
Chain D 93–208（116 aa） Fragment：Fadd DD, UNP residues 93-208
Not recorded 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
3EZQ Crystal Structure of the Fas/FADD Death Domain Complex Deposited 2008-10-23 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain F 93–208（116 aa） Fragment：Fadd DD, UNP residues 93-208
Chain H 93–208（116 aa） Fragment：Fadd DD, UNP residues 93-208
Not recorded 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
3EZQ Crystal Structure of the Fas/FADD Death Domain Complex Deposited 2008-10-23 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 3 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain J 93–208（116 aa） Fragment：Fadd DD, UNP residues 93-208
Chain L 93–208（116 aa） Fragment：Fadd DD, UNP residues 93-208
Not recorded 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
3EZQ Crystal Structure of the Fas/FADD Death Domain Complex Deposited 2008-10-23 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 4 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain N 93–208（116 aa） Fragment：Fadd DD, UNP residues 93-208
Chain P 93–208（116 aa） Fragment：Fadd DD, UNP residues 93-208
Not recorded 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
3OQ9 Structure of the FAS/FADD death domain assembly Deposited 2010-09-02 Different construct Different mutation/modification Different oligomeric state Different experimental method 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 method 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 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 method 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 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）
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 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 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 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 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 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 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 19 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FADD_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–83； UniProt 1–83

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 1a1w

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1a1w
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1a1w
Deposition date deposition_date1997-12-18
Structure title titleFADD DEATH EFFECTOR DOMAIN, F25Y MUTANT, NMR MINIMIZED AVERAGE STRUCTURE
Keywords keywordsAPOPTOSIS, DEATH EFFECTOR DOMAIN; APOPTOSIS
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier13.96 Å
Radius of gyration Rg (electron density) rg_electron12.11 Å
Forward intensity I(0) i02034790.00
Molecular weight molecular_weight9546.0 kDa
Excluded volume excluded_volume11992 ų
Envelope volume envelope_volume14114 ų
Hydration-shell volume shell_volume9986 ų
Envelope diameter envelope_diameter43.3 Å
Shell Rg shell_rg17.71 Å
Envelope Rg envelope_rg12.53 Å
Shape Rg shape_rg12.08 Å
Total Rg total_rg13.67 Å
Total atoms total_atoms1360
Residues n_residues83
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax44.6 Å
Rg (real space) rg_real13.85 Å
Rg uncertainty (real space) rg_real_error0.33 Å
I(0) (real space) i0_real2.0350e+06
I(0) uncertainty (real space) i0_real_error2.0210e+04
Rg (reciprocal space) rg_reciprocal13.86 Å
I(0) (reciprocal space) i0_reciprocal2035000.0000
Solution quality estimate total_estimate0.8649
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary19.2 Å
Skewness Skewness skewness0.066
Kurtosis Kurtosis kurtosis-0.236
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha750300.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.767; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.985; Smooth: 0.958
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1a1wa_
Class classa — All alpha proteins
Fold Fold folda.77 — DEATH domain
Superfamily Superfamily superfamilya.77.1 — DEATH domain
Family Family familya.77.1.4 — DEATH effector domain, DED

CATH v4.4 (1 domains)

Domain ID domain_id1a1wA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology533 — Death Domain, Fas
Homologous superfamily homologous superfamily10 — Death Domain, Fas
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8. Citations (1)

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9. Files and Curves (10)