Research workbench
TMEM106B filaments with fold I-D from multiple system atrophy (case 18)
Analyse TMEM106B filaments with fold I-D from multiple system atrophy (case 18) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7QVF
- Type
- protein
- Length
- 810 residues
- Chains
- 6
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transmembrane protein 106B
- UniProt
- Q9NUM4
- Pockets
- 8 · best druggability 0.53
Structure
electron microscopy · 1 distinct chain · 0% helix, 73% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | Transmembrane protein 106B | protein | 135 | 0% helix, 73% strand | Q9NUM4 |
Pockets
8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 254 | 0.53 | 0.76 | 28 | empty |
| 2 | 141 | 0.51 | 0.79 | 18 | empty |
| 3 | 129 | 0.50 | 0.78 | 18 | empty |
| 4 | 231 | 0.49 | 0.75 | 25 | empty |
| 5 | 86 | 0.48 | 0.82 | 19 | empty |
Interfaces
6 interfaces between chains.
- D–E · 5849 Ų buried · 182 hydrogen bonds · protein-protein
- B–C · 5843 Ų buried · 182 hydrogen bonds · protein-protein
- D–F · 5836 Ų buried · 184 hydrogen bonds · protein-protein
- A–B · 5829 Ų buried · 184 hydrogen bonds · protein-protein
- E–F · 72 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide (disulfide).
Compared structures
- 7QVF · TMEM106B filaments with Fold I-d from Multiple system atrophy (case 18) · the same entry in another collection · chain C against C, TM-score 1.00
- Q9NUM4 · AlphaFold monomer V2.0 prediction for transmembrane protein 106B (Q9NUM4) · a predicted model of the same protein · chain A against A, TM-score 0.19
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 Q9NUM4
- Elsewhere: RCSB PDB 7QVF · PDBe 7QVF · UniProt Q9NUM4
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