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Protein Structures and Oligomeric States

Enter a protein name, UniProt accession or PDB ID. Name searches ask you to confirm the protein identity before related structures are queried.

Current Protein Identity：Q13158 New Search
17PDB entries
20Biological assembly
122chain/assembly records
Main Difference Dimensions in This Set
Different construct Different mutation/modification Different assembly state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics

Difference tags compare only the current result set; every original PDB and assembly record remains separate.

Related-Structure Differences

Each row represents one biological assembly in one PDB entry; multiple monomers of the same protein are listed separately.

PDB Entry Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Experimental Method Experimental Conditions Structure Quality
1A1W FADD DEATH EFFECTOR DOMAIN, F25Y MUTANT, NMR MINIMIZED AVERAGE STRUCTURE Deposited 1997-12-18 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
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 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
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 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
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 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
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 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
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 Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
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 Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
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 Assembly 3 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
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 Assembly 4 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
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 Assembly 1 Protein heterocomplex Heteromer；Protein × 10 PDB declaration: decameric（10） Consistent with protein count
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 Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
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 Assembly 1 Protein heterocomplex Heteromer；Protein × 10 PDB declaration: decameric（10） Consistent with protein count
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 Assembly 1 Protein heterocomplex Heteromer；Protein × 10 PDB declaration: decameric（10） Consistent with protein count
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 Assembly 1 Protein heterocomplex Heteromer；Protein × 10 PDB declaration: decameric（10） Consistent with protein count
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 Assembly 1 Protein heterocomplex Heteromer；Protein × 11 PDB declaration: 11-meric（11） Consistent with protein count
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 Assembly 1 Protein homooligomer Homooligomer；Protein × 18 PDB declaration: 18-meric（18） Consistent with protein count
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 Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric（24） Consistent with protein count
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 Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: 12-meric（12） Consistent with protein count
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 Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric（24） Consistent with protein count
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 Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric（24） Consistent with protein count
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

This page presents structural evidence recorded in PDB/mmCIF.“No recorded non-water small molecule” does not prove that the experimental sample was ligand-free; experimental conditions belong to the PDB experiment, while ligands and copy counts are shown for each biological assembly.