MolNFT v1 · #185907 · protein
In vitro assembled tau filaments with structures like paired helical filaments from ALZHEIMER'S disease
7QL4 · Microtubule-associated protein tau: “In vitro assembled tau filaments with structures like paired helical filaments from ALZHEIMER'S disease”. Electron microscopy. MolNFT v1 #185907 on GenesisL1: 3D structure, binding sites and…
- PDB
- 7QL4
- Type
- protein
- Length
- 456 residues
- Chains
- 6
- 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, 63% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, F, B, C, D, E | Microtubule-associated protein tau | protein | 76 | 0% helix, 63% strand | P10636 |
Interfaces
12 interfaces between chains.
- B–D · 3141 Ų buried · 84 hydrogen bonds · protein-protein
- C–E · 3138 Ų buried · 86 hydrogen bonds · protein-protein
- A–D · 3133 Ų buried · 85 hydrogen bonds · protein-protein
- F–E · 3126 Ų buried · 88 hydrogen bonds · protein-protein
- B–C · 227 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 7QL4 · in vitro assembled tau filaments with structures like Paired Helical Filaments from… · the same entry in another collection · chain D against D, 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 7QL4 · PDBe 7QL4 · UniProt P10636
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