Research workbench
AlphaFold monomer V2.0 prediction for nuclear pore complex protein NUP107 (Q9V466)
Analyse AlphaFold monomer V2.0 prediction for nuclear pore complex protein NUP107… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9V466
- Type
- protein
- Length
- 845 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xF8cD1d8d93E9783063700De244A6e3cf6A195579
- Molecule
- Nuclear pore complex protein NUP107
- UniProt
- Q9V466
- Pockets
- 8 · best druggability 0.79
Structure
1 distinct chain · 65% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nuclear pore complex protein NUP107 | protein | 845 | 65% helix, 0% strand | Q9V466 |
Pockets
8 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 563 | 0.79 | 0.85 | 54 | empty |
| 2 | 240 | 0.65 | 0.83 | 31 | empty |
| 3 | 67 | 0.65 | 0.93 | 16 | empty |
| 4 | 265 | 0.51 | 0.74 | 36 | empty |
| 5 | 128 | 0.44 | 0.77 | 26 | 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 Q9V466
- Elsewhere: UniProt Q9V466 · AlphaFold DB Q9V466
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