Research workbench
In vitro assembled 258-391 tau filaments with sodium azide, (41A)
Analyse In vitro assembled 258-391 tau filaments with sodium azide, (41A) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7QKH
- Type
- protein
- Length
- 204 residues
- Chains
- 6
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Microtubule-associated protein tau
- UniProt
- P10636
Structure
electron microscopy · 2 distinct chains · 0% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, D | Microtubule-associated protein tau | protein | 34 | 0% helix, 50% strand | P10636 |
| G, C, E | Microtubule-associated protein tau | protein | 34 | 0% helix, 32% strand | P10636 |
Interfaces
12 interfaces between chains.
- A–D · 1448 Ų buried · 31 hydrogen bonds · protein-protein
- A–B · 1409 Ų buried · 31 hydrogen bonds · protein-protein
- G–E · 1397 Ų buried · 29 hydrogen bonds · protein-protein
- G–C · 1392 Ų buried · 28 hydrogen bonds · protein-protein
- A–E · 774 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 7QKH · In vitro assembled 258-391 tau filaments with sodium azide, (41a) · the same entry in another collection · chain A against A, 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 7QKH · PDBe 7QKH · UniProt P10636
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