Research workbench
In vitro assembled tau filaments with structures like paired helical filaments from ALZHEIMER'S disease
Analyse In vitro assembled tau filaments with structures like paired helical filaments… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7QL4
- Type
- protein
- Length
- 456 residues
- Chains
- 6
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Microtubule-associated protein tau
- UniProt
- P10636
Structure
electron microscopy · 1 distinct chain · 0% helix, 63% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, F, B, C, D, E | Microtubule-associated protein tau | protein | 76 | 0% helix, 63% strand | P10636 |
Interfaces
12 interfaces between chains.
- B–D · 3141 Ų buried · 84 hydrogen bonds · protein-protein
- C–E · 3138 Ų buried · 86 hydrogen bonds · protein-protein
- A–D · 3133 Ų buried · 85 hydrogen bonds · protein-protein
- F–E · 3126 Ų buried · 88 hydrogen bonds · protein-protein
- B–C · 227 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 7QL4 · in vitro assembled tau filaments with structures like Paired Helical Filaments from… · the same entry in another collection · chain D against D, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P10636
- Elsewhere: RCSB PDB 7QL4 · PDBe 7QL4 · UniProt P10636
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