9o6v

Recombinant AD PHF complexed with SW-MK-NBD (PHF2)

Method: ELECTRON MICROSCOPY Dmax: 139.0 Å Quality: REASONABLE

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 F; UniProt 622–696 Chain G; UniProt 622–696 Chain H; UniProt 622–696 Chain I; UniProt 622–696 Chain J; UniProt 622–696 Chain N; UniProt 622–696 Chain O; UniProt 622–696 Chain P; UniProt 622–696 Chain Y; UniProt 622–696 Chain Z; UniProt 622–696 Not recorded A1B91 7-nitro-N-[2-(2-{[(3P)-3-(1H-pyrrolo[2,3-c]pyridin-1-yl)isoquinolin-7-yl]oxy}ethoxy)ethyl]-2,1,3-benzoxadiazol-4-amine × 10 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4;10 mM Phosphate buffer, pH 7.4, with 10 mM DTT and 200 mM MgCl2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.72 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 F; PDBConstruct 1–75; UniProt 622–696 Author chain G; PDBConstruct 1–75; UniProt 622–696 Author chain H; PDBConstruct 1–75; UniProt 622–696 Author chain I; PDBConstruct 1–75; UniProt 622–696 Author chain J; PDBConstruct 1–75; UniProt 622–696 Author chain N; PDBConstruct 1–75; UniProt 622–696 Author chain O; PDBConstruct 1–75; UniProt 622–696 Author chain P; PDBConstruct 1–75; UniProt 622–696 Author chain Y; PDBConstruct 1–75; UniProt 622–696 Author chain Z; PDBConstruct 1–75; UniProt 622–696

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 9o6v

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9o6v
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9o6v
Deposition date deposition_date2025-04-14
Structure title titleRecombinant AD PHF complexed with SW-MK-NBD (PHF2)
Keywords keywordsMK-6240 PET Ligand, AD PHF, PROTEIN FIBRIL, SW-MK-NBD, Amyloid Dye; PROTEIN FIBRIL
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier35.76
Radius of gyration Rg (electron density) rg_electron37.28
Forward intensity I(0) i0116824000.00
Molecular weight molecular_weight86850.0 kDa
Excluded volume excluded_volume109040 ų
Envelope volume envelope_volume143560 ų
Hydration-shell volume shell_volume35480 ų
Envelope diameter envelope_diameter143.8
Shell Rg shell_rg38.70
Envelope Rg envelope_rg37.90
Shape Rg shape_rg37.69
Total Rg total_rg35.97
Total atoms total_atoms12340
Residues n_residues750
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 dmax139.0
Rg (real space) rg_real36.32
Rg uncertainty (real space) rg_real_error1.61
I(0) (real space) i0_real1.1680e+08
I(0) uncertainty (real space) i0_real_error2.1060e+06
Rg (reciprocal space) rg_reciprocal35.97
I(0) (reciprocal space) i0_reciprocal116800000.0000
Solution quality estimate total_estimate0.7472
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary34.8
Skewness Skewness skewness0.721
Kurtosis Kurtosis kurtosis0.147
Angular range angular_range— – 0.2200 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha10650000.0000
Real-space data points n_real_points45
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.461; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.374; Smooth: 0.954

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)