Research workbench
In vitro assembled 305-379 tau filaments (27A)
Analyse In vitro assembled 305-379 tau filaments (27A) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7QKZ
- Type
- protein
- Length
- 99 residues
- Chains
- 9
- 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, 45% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B, A, C, D, E, F, G, H, I | Microtubule-associated protein tau | protein | 11 | 0% helix, 45% strand | P10636 |
Interfaces
21 interfaces between chains.
- G–H · 504 Ų buried · 11 hydrogen bonds · protein-protein
- B–C · 504 Ų buried · 12 hydrogen bonds · protein-protein
- G–I · 502 Ų buried · 12 hydrogen bonds · protein-protein
- D–F · 499 Ų buried · 12 hydrogen bonds · protein-protein
- B–A · 498 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 7QKZ · In vitro assembled 305-379 tau filaments (27a) · the same entry in another collection · chain B against B, 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 7QKZ · PDBe 7QKZ · UniProt P10636
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