Research workbench
Narrow Pick Filament from Pick's disease brain
Analyse Narrow Pick Filament from Pick'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
- 6GX5
- Type
- protein
- Length
- 282 residues
- Chains
- 3
- Method
- electron microscopy
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 3.2
- Source
- Homo sapiens
- Molecule
- Microtubule-associated protein tau
- UniProt
- P10636
- Pockets
- 1 · best druggability 0.53
Structure
electron microscopy · resolution 3.2 · 1 distinct chain · 0% helix, 65% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Microtubule-associated protein tau | protein | 94 | 0% helix, 65% strand | P10636 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 140 | 0.53 | 0.81 | 24 | empty |
Interfaces
3 interfaces between chains.
- A–C · 4056 Ų buried · 123 hydrogen bonds · protein-protein
- A–B · 4056 Ų buried · 123 hydrogen bonds · protein-protein
- B–C · 52 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
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 6GX5 · PDBe 6GX5 · UniProt P10636
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