SAXSdb — 3oq9

▼

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

Tumor necrosis factor receptor superfamily member 6

Mus musculus

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 223–308 Chain B； UniProt 223–308 Chain C； UniProt 223–308 Chain D； UniProt 223–308 Chain E； UniProt 223–308	Fragment：UNP residues 223-308	Protein FADD × 5 （Q13158）	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

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 3OQ9	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2NA6 Transmembrane domain of mouse Fas/CD95 death receptor Deposited 2015-12-21	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 167–193（27 aa） Fragment：Helical transmembrane residues 167-193 Chain B 167–193（27 aa） Fragment：Helical transmembrane residues 167-193 Chain C 167–193（27 aa） Fragment：Helical transmembrane residues 167-193	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] Mouse 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] Mouse 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] Mouse Fas Transmembrane Domain, 0.5 mM [U-15% 13C] Mouse 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

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	TNR6_MOUSE
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–86； UniProt 223–308 Author chain B； PDBConstruct 1–86； UniProt 223–308 Author chain C； PDBConstruct 1–86； UniProt 223–308 Author chain D； PDBConstruct 1–86； UniProt 223–308 Author chain E； PDBConstruct 1–86； UniProt 223–308

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 × 10 PDB declaration: decameric（10） Consistent with protein copy count	Chain H； UniProt 93–184 Chain I； UniProt 93–184 Chain J； UniProt 93–184 Chain K； UniProt 93–184 Chain L； UniProt 93–184	Fragment：UNP residues 93-184	Tumor necrosis factor receptor superfamily member 6 × 5 （P25446）	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

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 3OQ9	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 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 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 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 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 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
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 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 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 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 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
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 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 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 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 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	2
Chains and sequence ranges	Author chain H； PDBConstruct 1–92； UniProt 93–184 Author chain I； PDBConstruct 1–92； UniProt 93–184 Author chain J； PDBConstruct 1–92； UniProt 93–184 Author chain K； PDBConstruct 1–92； UniProt 93–184 Author chain L； PDBConstruct 1–92； UniProt 93–184

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.

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id	3oq9
Deposition date deposition_date	2010-09-02
Structure title title	Structure of the FAS/FADD death domain assembly
Keywords keywords	APOPTOSIS, DISC, FAS, FADD; APOPTOSIS
Experimental Method method	X-RAY DIFFRACTION

▼

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

Radius of gyration Rg (Guinier) rg_guinier	30.17 Å
Radius of gyration Rg (electron density) rg_electron	29.11 Å
Forward intensity I(0) i0	185624000.00
Molecular weight molecular_weight	103630.0 kDa
Excluded volume excluded_volume	128420 Å³
Envelope volume envelope_volume	169330 Å³
Hydration-shell volume shell_volume	46417 Å³
Envelope diameter envelope_diameter	101.5 Å
Shell Rg shell_rg	37.91 Å
Envelope Rg envelope_rg	29.12 Å
Shape Rg shape_rg	29.11 Å
Total Rg total_rg	29.94 Å
Total atoms total_atoms	7255
Residues n_residues	890
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

▼

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

Maximum dimension Dmax dmax	95.2 Å
Rg (real space) rg_real	29.96 Å
Rg uncertainty (real space) rg_real_error	0.41 Å
I(0) (real space) i0_real	1.8560e+08
I(0) uncertainty (real space) i0_real_error	2.6030e+06
Rg (reciprocal space) rg_reciprocal	30.05 Å
I(0) (reciprocal space) i0_reciprocal	185600000.0000
Solution quality estimate total_estimate	0.8903
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	39.5 Å
Skewness Skewness skewness	0.123
Kurtosis Kurtosis kurtosis	-0.424
Angular range angular_range	— – 0.2650 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	55460000.0000
Real-space data points n_real_points	54
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.866; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.976; Smooth: 0.996

▶

5. Crystallography and Experiment 5. Crystallography & Experiment

▶

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Description description	Tumor necrosis factor receptor superfamily member 6
Molecular weight formula_weight	10162.7 kDa
Source method src_method	man
Copy count entity_count	5

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E
Atom count atom_count	7255

KYIPRIAEDMTIQEAKKFARENNIKEGKIDEIMHDSIQDTAEQKVQLLLCWYQSHGKSDAYQDLIKGLKKAECRRTLDKFQDMVQK

来源 Source

来源生物 organism	Mus musculus
通用名 common_name	mouse
NCBI Class编号 ncbi_taxonomy_id	10090
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	Protein FADD
Molecular weight formula_weight	11685.2 kDa
Source method src_method	man
Copy count entity_count	5

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	H,I,J,K,L

GEEDLCAAFNVICDNVGKDWRRLARQLKVSDTKIDSIEDRYPRNLTERVRESLRIWKNTEKENATVAHLVGALRSCQMNLVADLVQEVQQARLEHHHHHH

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

▶

8. Citations (1)

▶

Unit-cell length a length_a	135.204 Å
Unit-cell length b length_b	144.447 Å
Unit-cell length c length_c	131.574 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	40

Space group space_group	C 2 2 21
Space-group number int_tables_number	20
Crystal system crystal_system	—

Resolution resolution	6.800 Å
Low-resolution limit resolution_low	20.000 Å
R factor r_factor	—
R_work r_work	0.3434
R_free r_free	0.3542

fit	/app/data/saxs_computation/oq/3oq9/3oq9.fit
pddf	/app/data/pr_computation/oq/3oq9/3oq9.pr.out
profile	/app/data/saxs_computation/oq/3oq9/3oq9.dat

Structure of the FAS/FADD death domain assembly

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

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)