MolNFT v1 · #190470 · protein
Cryo-EM structure of the TMEM106B fibril from normal elder
7X83 · Transmembrane protein 106B: “Cryo-EM structure of the TMEM106B fibril from normal elder”. Electron microscopy, 3 pockets (best druggability 0.50). MolNFT v1 #190470 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7X83
- Type
- protein
- Length
- 405 residues
- Chains
- 3
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transmembrane protein 106B
- UniProt
- Q9NUM4
- Pockets
- 3 · best druggability 0.50
Structure
electron microscopy · 1 distinct chain · 0% helix, 51% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B, A, C | Transmembrane protein 106B | protein | 135 | 0% helix, 51% strand | Q9NUM4 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 227 | 0.50 | 0.76 | 27 | empty |
| 2 | 100 | 0.50 | 0.81 | 15 | empty |
| 3 | 105 | 0.48 | 0.80 | 17 | empty |
Interfaces
3 interfaces between chains.
- B–C · 6158 Ų buried · 175 hydrogen bonds · protein-protein
- B–A · 6155 Ų buried · 174 hydrogen bonds · protein-protein
- A–C · 353 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
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 7X83 · PDBe 7X83 · UniProt Q9NUM4
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