Research workbench
Straight filament from sporadic Alzheimer's disease brain
Analyse Straight filament from sporadic Alzheimer's disease brain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6HRF
- Type
- protein
- Length
- 462 residues
- Chains
- 6
- Method
- electron microscopy
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 3.3
- Source
- Homo sapiens
- Molecule
- Microtubule-associated protein tau
- UniProt
- P10636
- Pockets
- 2 · best druggability 0.35
Structure
electron microscopy · resolution 3.3 · 1 distinct chain · 0% helix, 45% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | Microtubule-associated protein tau | protein | 77 | 0% helix, 45% strand | P10636 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 64 | 0.35 | 0.77 | 15 | empty |
| 2 | 57 | 0.33 | 0.77 | 19 | empty |
Interfaces
9 interfaces between chains.
- C–E · 3257 Ų buried · 85 hydrogen bonds · protein-protein
- A–C · 3254 Ų buried · 85 hydrogen bonds · protein-protein
- D–F · 3227 Ų buried · 78 hydrogen bonds · protein-protein
- B–D · 3216 Ų buried · 71 hydrogen bonds · protein-protein
- E–F · 107 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 6HRF · Straight filament from sporadic ALZHEIMER'S disease brain · the same entry in another collection · chain C against C, 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 0.27
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 6HRF · PDBe 6HRF · UniProt P10636
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