10ik

S305I Frontotemporal Lobar Degeneration (FTLD) type II tau filament

Method: ELECTRON MICROSCOPY Dmax: 110.3 Å Quality: GOOD

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

Microtubule-associated protein tau

Homo sapiens

UniProt P10636

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 homooligomer Homooligomer Protein × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain A; UniProt 590–696 Chain B; UniProt 590–696 Chain C; UniProt 590–696 Chain D; UniProt 590–696 Chain E; UniProt 590–696 Chain F; UniProt 590–696 Chain G; UniProt 590–696 Chain H; UniProt 590–696 Chain I; UniProt 590–696 Chain J; UniProt 590–696 Mutation:S305I No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 Å

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.

248 other PDB entries and 270 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TAU_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–107; UniProt 590–696 Author chain B; PDBConstruct 1–107; UniProt 590–696 Author chain C; PDBConstruct 1–107; UniProt 590–696 Author chain D; PDBConstruct 1–107; UniProt 590–696 Author chain E; PDBConstruct 1–107; UniProt 590–696 Author chain F; PDBConstruct 1–107; UniProt 590–696 Author chain G; PDBConstruct 1–107; UniProt 590–696 Author chain H; PDBConstruct 1–107; UniProt 590–696 Author chain I; PDBConstruct 1–107; UniProt 590–696 Author chain J; PDBConstruct 1–107; UniProt 590–696

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 10ik

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 10ik
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2. Structure Basics 2. Structure Basics

Entry ID entry_id10ik
Deposition date deposition_date2026-01-21
Structure title titleS305I Frontotemporal Lobar Degeneration (FTLD) type II tau filament
Keywords keywordstau, MAPT, FTD, FTLD, amyloid, neurodegeneration, PROTEIN FIBRIL; PROTEIN FIBRIL
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier33.22
Radius of gyration Rg (electron density) rg_electron32.84
Forward intensity I(0) i0203840000.00
Molecular weight molecular_weight115310.0 kDa
Excluded volume excluded_volume145280 ų
Envelope volume envelope_volume178920 ų
Hydration-shell volume shell_volume44726 ų
Envelope diameter envelope_diameter119.5
Shell Rg shell_rg40.35
Envelope Rg envelope_rg32.98
Shape Rg shape_rg32.82
Total Rg total_rg33.47
Total atoms total_atoms16670
Residues n_residues1070
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −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

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

Maximum dimension Dmax dmax110.3
Rg (real space) rg_real33.19
Rg uncertainty (real space) rg_real_error0.72
I(0) (real space) i0_real2.0380e+08
I(0) uncertainty (real space) i0_real_error2.9200e+06
Rg (reciprocal space) rg_reciprocal33.21
I(0) (reciprocal space) i0_reciprocal203800000.0000
Solution quality estimate total_estimate0.8964
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary39.1
Skewness Skewness skewness0.282
Kurtosis Kurtosis kurtosis-0.469
Angular range angular_range— – 0.2400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha21930000.0000
Real-space data points n_real_points49
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.900; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.983; Smooth: 0.967

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)