Research workbench
Straight filament from ALZHEIMER'S disease human brain tissue
Analyse Straight filament from ALZHEIMER'S disease human brain tissue in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6VI3
- Type
- protein
- Length
- 154 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Microtubule-associated protein tau
- UniProt
- P10636
- Ligands
- GLY
Structure
electron microscopy · 1 distinct chain · 0% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| E, F | Microtubule-associated protein tau | protein | 77 | 0% helix, 0% strand | P10636 |
Ligands and binding sites
- GLY · Glycine · ligand · 2 copies · chains E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- E–F · 114 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
- 6VI3 · Straight Filament from Alzheimer's Disease Human Brain Tissue · the same entry in another collection · chain E against E, TM-score 1.00
- P10636 · AlphaFold monomer V2.0 prediction for microtubule-associated protein tau (P10636) · a predicted model of the same protein · chain F 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 6VI3 · PDBe 6VI3 · UniProt P10636
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