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7nrt

Conformation 2 of straight filament from primary age-related tauopathy brain

Method: ELECTRON MICROSCOPY
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Microtubule-associated protein tau

OrganismNot specified

UniProt P10636

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein homooligomer Homooligomer Protein 10 No other associated polymer Consistent with protein count

Other States of the Same Protein in the Database

Monomer
2mz7 5n5a 5n5b 8p34 9eo7 9eoe 9mr8

7 assemblies

Homodimer
6vhl 6vi3 9eo9

3 assemblies

Homotetramer
9gg1

1 assemblies

Other homooligomers
10ij 10ik 22jy 3ovl 4np8 5o3l 5o3o 5o3t 5v5b 5v5b 6gx5 6hre

206 assemblies; showing the first 12

Heteromeric or nucleic-acid complex
1i8h 4fl5 4tqe 4y5i 5mo3 5mp1 5mp1 5mp1 5mp1 5mp5 5mp5 5mp5

54 assemblies; showing the first 12

View Construct and Data Evidence
UniProt name TAU_HUMAN
Isoform P10636-8
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–441； UniProt 1–441 Author chain B； PDBConstruct 1–441； UniProt 1–441 Author chain C； PDBConstruct 1–441； UniProt 1–441 Author chain D； PDBConstruct 1–441； UniProt 1–441 Author chain E； PDBConstruct 1–441； UniProt 1–441 Author chain F； PDBConstruct 1–441； UniProt 1–441 Author chain G； PDBConstruct 1–441； UniProt 1–441 Author chain H； PDBConstruct 1–441； UniProt 1–441 Author chain I； PDBConstruct 1–441； UniProt 1–441 Author chain J； PDBConstruct 1–441； UniProt 1–441

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_id7nrt
Deposition date deposition_date2021-03-04
Structure title titleConformation 2 of straight filament from primary age-related tauopathy brain
Keywords keywordsTau filament, PROTEIN FIBRIL; PROTEIN FIBRIL
Experimental Method methodELECTRON MICROSCOPY
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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

7nrt__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

7nrt__assembly_1__model_1 | I(q)

10-2 10-1 106 107 108 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

7nrt__assembly_1__model_1 | P(r) · Pending

The new assembly/model P(r) has not been calculated yet This placeholder does not display legacy data r (Angstrom) P(r)
P(r) will be calculated and displayed separately for the same assembly/model.
Rg（Guinier）36.59 Å
Rg (electron density)36.70 Å
Total Rg36.82 Å
Atom count5870
Residues770
Excluded volume104670 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 7nrt__assembly_1__model_1 decameric （10） Success 4.1.3-1-20251215 (887e7ef) View Download
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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (1)

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7. Citations (1)