Research workbench
AlphaFold monomer V2.0 prediction for nuclear pore complex protein NUP133 (F1QNV4)
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
- F1QNV4
- Type
- protein
- Length
- 1,136 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9188600a0FCa2914254C94299b1bd9721Bc4D500
- Molecule
- Nuclear pore complex protein NUP133
- UniProt
- F1QNV4
- Pockets
- 13 · best druggability 0.80
Structure
1 distinct chain · 45% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nuclear pore complex protein NUP133 | protein | 1136 | 45% helix, 15% strand | F1QNV4 |
Pockets
13 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 983 | 0.80 | 0.81 | 93 | empty |
| 2 | 753 | 0.67 | 0.75 | 76 | empty |
| 3 | 251 | 0.52 | 0.76 | 34 | empty |
| 4 | 123 | 0.50 | 0.80 | 20 | empty |
| 5 | 66 | 0.44 | 0.81 | 13 | 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 F1QNV4
- Elsewhere: UniProt F1QNV4 · AlphaFold DB F1QNV4
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