Structure analysis

In vitro assembled 258-391 tau filaments with heparan sulfate, 700 rpm (40a)

Electron Microscopy
2.27Å resolution
Source organism: Homo sapiens
Assembly composition:
homo trimer (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: homo trimer
Accessible surface area: 9514.34 Å2
Buried surface area: 8519.3 Å2
Dissociation area: 4,259.65 Å2
Dissociation energy (ΔGdiss): 63.43 kcal/mol
Dissociation entropy (TΔSdiss): 22.63 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-145400

Macromolecules

Chains: A, B, C
Length: 441 amino acids
Theoretical weight: 45.92 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P10636 (Residues: 1-758; Coverage: 58%)
  • Best match: P10636-8 (Residues: 1-441)
Gene names: MAPT, MAPTL, MTBT1, TAU
Pfam: Tau and MAP protein, tubulin-binding repeat
InterPro:

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