Research workbench
AlphaFold monomer V2.0 prediction for nuclear pore complex protein 14 (Q17602)
Analyse AlphaFold monomer V2.0 prediction for nuclear pore complex protein 14 (Q17602) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q17602
- Type
- protein
- Length
- 1,390 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xB44F19a0cb161828322eEEd13F55d4C3C34938d2
- Molecule
- Nuclear pore complex protein 14
- UniProt
- Q17602
- Pockets
- 9 · best druggability 0.81
Structure
1 distinct chain · 18% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nuclear pore complex protein 14 | protein | 1390 | 18% helix, 14% strand | Q17602 |
Pockets
9 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 967 | 0.81 | 0.82 | 74 | empty |
| 2 | 445 | 0.80 | 0.88 | 48 | empty |
| 3 | 398 | 0.67 | 0.79 | 32 | empty |
| 4 | 203 | 0.57 | 0.80 | 20 | empty |
| 5 | 157 | 0.50 | 0.78 | 17 | 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 Q17602
- Elsewhere: UniProt Q17602 · AlphaFold DB Q17602
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