Research workbench
Cryo-EM structure of heparin-induced 2N4R tau jagged filaments
Analyse Cryo-EM structure of heparin-induced 2N4R tau jagged filaments in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6QJP
- Type
- protein
- Length
- 105 residues
- Chains
- 3
- Method
- electron microscopy
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 3.5
- Source
- Homo sapiens
- Molecule
- Microtubule-associated protein tau
- UniProt
- P10636
Structure
electron microscopy · resolution 3.5 · 1 distinct chain · 0% helix, 71% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, B | Microtubule-associated protein tau | protein | 35 | 0% helix, 71% strand | P10636 |
Interfaces
3 interfaces between chains.
- A–B · 1608 Ų buried · 50 hydrogen bonds · protein-protein
- A–C · 1605 Ų buried · 53 hydrogen bonds · protein-protein
- C–B · 41 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 6QJP · Cryo-EM structure of heparin-induced 2N4R tau jagged filaments · the same entry in another collection · chain A against A, TM-score 1.00
- P10636 · AlphaFold monomer V2.0 prediction for microtubule-associated protein tau (P10636) · a predicted model of the same protein · chain A against A, TM-score 0.30
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 6QJP · PDBe 6QJP · UniProt P10636
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