Research workbench
AlphaFold monomer V2.0 prediction for nuclear pore complex protein NUP133 (F4IGA5)
Analyse AlphaFold monomer V2.0 prediction for nuclear pore complex protein NUP133… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- F4IGA5
- Type
- protein
- Length
- 1,285 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x59018c174d1Ecad02850b8c56eDC5A53F1C2d4c5
- Molecule
- Nuclear pore complex protein NUP133
- UniProt
- F4IGA5
- Pockets
- 16 · best druggability 0.85
Structure
1 distinct chain · 42% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nuclear pore complex protein NUP133 | protein | 1285 | 42% helix, 14% strand | F4IGA5 |
Pockets
16 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1012 | 0.85 | 0.86 | 90 | empty |
| 2 | 1005 | 0.76 | 0.79 | 100 | empty |
| 3 | 1157 | 0.74 | 0.77 | 84 | empty |
| 4 | 656 | 0.64 | 0.74 | 78 | empty |
| 5 | 67 | 0.53 | 0.87 | 11 | 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 F4IGA5
- Elsewhere: UniProt F4IGA5 · AlphaFold DB F4IGA5
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