Research workbench
AlphaFold monomer V2.0 prediction for trafficking protein particle complex subunit 14 (E7F240)
Analyse AlphaFold monomer V2.0 prediction for trafficking protein particle complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- E7F240
- Type
- protein
- Length
- 595 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xbb2F1C7CB3A1eeFAc24fCa72cc627162D5413FD7
- Molecule
- Trafficking protein particle complex subunit 14
- UniProt
- E7F240
- Pockets
- 6 · best druggability 0.65
Structure
1 distinct chain · 10% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Trafficking protein particle complex subunit 14 | protein | 595 | 10% helix, 37% strand | E7F240 |
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 613 | 0.65 | 0.75 | 42 | empty |
| 2 | 275 | 0.52 | 0.75 | 38 | empty |
| 3 | 137 | 0.39 | 0.73 | 31 | empty |
| 4 | 73 | 0.38 | 0.78 | 17 | empty |
| 5 | 59 | 0.32 | 0.76 | 15 | empty |
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 E7F240
- Elsewhere: UniProt E7F240 · AlphaFold DB E7F240
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