Research workbench
AlphaFold monomer V2.0 prediction for nuclear pore complex protein NUP160 homolog (Q9VKJ3)
Analyse AlphaFold monomer V2.0 prediction for nuclear pore complex protein NUP160… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9VKJ3
- Type
- protein
- Length
- 1,411 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xf5A29B7351cEFe79Ad61F800C493687C2C155475
- Molecule
- Nuclear pore complex protein NUP160 homolog
- UniProt
- Q9VKJ3
- Pockets
- 19 · best druggability 0.82
Structure
1 distinct chain · 49% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nuclear pore complex protein NUP160 homolog | protein | 1411 | 49% helix, 15% strand | Q9VKJ3 |
Pockets
19 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1120 | 0.82 | 0.83 | 98 | empty |
| 2 | 1188 | 0.77 | 0.79 | 77 | empty |
| 3 | 541 | 0.71 | 0.80 | 63 | empty |
| 4 | 454 | 0.66 | 0.78 | 33 | empty |
| 5 | 113 | 0.57 | 0.84 | 24 | 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 Q9VKJ3
- Elsewhere: UniProt Q9VKJ3 · AlphaFold DB Q9VKJ3
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