SAXSdb — 1ddf

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

FAS

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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain A； UniProt 218–335	Not recorded	No other associated polymer	SOLUTION NMR NMR measurement conditions：pH 4	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 1DDF	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2NA7 Transmembrane domain of human Fas/CD95 death receptor Deposited 2015-12-21	Different construct Different mutation/modification Different oligomeric state Different experimental conditions	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 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 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
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 A 223–335（113 aa） Fragment：Fas DD, UNP residues 223-335 Chain C 223–335（113 aa） Fragment：Fas DD, UNP residues 223-335	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 E 223–335（113 aa） Fragment：Fas DD, UNP residues 223-335 Chain G 223–335（113 aa） Fragment：Fas DD, UNP residues 223-335	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 I 223–335（113 aa） Fragment：Fas DD, UNP residues 223-335 Chain K 223–335（113 aa） Fragment：Fas DD, UNP residues 223-335	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 M 223–335（113 aa） Fragment：Fas DD, UNP residues 223-335 Chain O 223–335（113 aa） Fragment：Fas DD, UNP residues 223-335	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
3THM Crystal structure of Fas receptor extracellular domain in complex with Fab EP6b_B01 Deposited 2011-08-19	Different construct Different oligomeric state Different ligand/ion Different experimental method 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 oligomeric state Different ligand/ion Different experimental method 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 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 9 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 2–119； UniProt 218–335

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_id	1ddf
Deposition date deposition_date	1996-11-08
Structure title title	FAS DEATH DOMAIN, NMR, MINIMIZED AVERAGE STRUCTURE
Keywords keywords	DEATH DOMAIN, APOPTOSIS, RECEPTOR, GLYCOPROTEIN, TRANSMEMBRANE; DEATH DOMAIN
Experimental Method method	SOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier	18.62 Å
Radius of gyration Rg (electron density) rg_electron	17.39 Å
Forward intensity I(0) i0	4369590.00
Molecular weight molecular_weight	14509.0 kDa
Excluded volume excluded_volume	18095 Å³
Envelope volume envelope_volume	23148 Å³
Hydration-shell volume shell_volume	12320 Å³
Envelope diameter envelope_diameter	62.2 Å
Shell Rg shell_rg	21.83 Å
Envelope Rg envelope_rg	17.80 Å
Shape Rg shape_rg	17.38 Å
Total Rg total_rg	18.30 Å
Total atoms total_atoms	2051
Residues n_residues	127
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	62.4 Å
Rg (real space) rg_real	18.68 Å
Rg uncertainty (real space) rg_real_error	0.49 Å
I(0) (real space) i0_real	4.3700e+06
I(0) uncertainty (real space) i0_real_error	5.5820e+04
Rg (reciprocal space) rg_reciprocal	18.67 Å
I(0) (reciprocal space) i0_reciprocal	4370000.0000
Solution quality estimate total_estimate	0.8768
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	18.8 Å
Skewness Skewness skewness	0.401
Kurtosis Kurtosis kurtosis	-0.391
Angular range angular_range	— – 0.4250 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	722700.0000
Real-space data points n_real_points	74
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.845; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.914; Smooth: 0.949

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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) 4 domains

SCOP 2.08 (3 domains)

Domain ID domain_id	d1ddfa1
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	d1ddfa2
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	d1ddfa3
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

CATH v4.4 (1 domains)

Domain ID domain_id	1ddfA00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	533 — Death Domain, Fas
Homologous superfamily homologous superfamily	10 — Death Domain, Fas

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8. Citations (1)

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Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 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	1

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	—

Description description	FAS
Molecular weight formula_weight	14535.5 kDa
Source method src_method	man
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	2051

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

FAS DEATH DOMAIN, NMR, MINIMIZED AVERAGE STRUCTURE

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

FAS

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

6. Entities and Polymers Entities & Polymers (1)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (3 domains)

CATH v4.4 (1 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

fit	/app/data/saxs_computation/dd/1ddf/1ddf.fit
pddf	/app/data/pr_computation/dd/1ddf/1ddf.pr.out
profile	/app/data/saxs_computation/dd/1ddf/1ddf.dat