Research workbench
AlphaFold monomer V2.0 prediction for nuclear pore complex protein NUP214 (F4I1T7)
Analyse AlphaFold monomer V2.0 prediction for nuclear pore complex protein NUP214… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- F4I1T7
- Type
- protein
- Length
- 1,819 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xb4D2d9c96b0D792d0b77e7147D724cc1F801ae58
- Molecule
- Nuclear pore complex protein NUP214
- UniProt
- F4I1T7
- Pockets
- 5 · best druggability 0.78
Structure
1 distinct chain · 11% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nuclear pore complex protein NUP214 | protein | 1819 | 11% helix, 11% strand | F4I1T7 |
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 938 | 0.78 | 0.81 | 79 | empty |
| 2 | 106 | 0.56 | 0.84 | 20 | empty |
| 3 | 59 | 0.45 | 0.83 | 14 | empty |
| 4 | 64 | 0.38 | 0.79 | 19 | empty |
| 5 | 80 | 0.36 | 0.76 | 23 | 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 F4I1T7
- Elsewhere: UniProt F4I1T7 · AlphaFold DB F4I1T7
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