Research workbench
AlphaFold monomer V2.0 prediction for nucleoporin NUP116/NSP116 (Q02630)
Analyse AlphaFold monomer V2.0 prediction for nucleoporin NUP116/NSP116 (Q02630) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q02630
- Type
- protein
- Length
- 1,113 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9073C46348542FfE4327c3F363F9B51B22058e75
- Molecule
- Nucleoporin NUP116/NSP116
- UniProt
- Q02630
- Pockets
- 4 · best druggability 0.61
Structure
1 distinct chain · 7% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nucleoporin NUP116/NSP116 | protein | 1113 | 7% helix, 5% strand | Q02630 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 556 | 0.61 | 0.75 | 66 | empty |
| 2 | 120 | 0.45 | 0.78 | 24 | empty |
| 3 | 164 | 0.41 | 0.73 | 26 | empty |
| 4 | 70 | 0.36 | 0.77 | 20 | empty |
Compared structures
- 3PBP · Structure of the yeast heterotrimeric NUP82-NUP159-NUP116 nucleoporin complex · an experimental structure of the same protein · chain A against B, TM-score 0.13
- 3PBP · Structure of the yeast heterotrimeric Nup82-Nup159-Nup116 nucleoporin complex · an experimental structure of the same protein · chain A against B, TM-score 0.13
- 2AIV · Multiple conformations in the ligand-binding site of the yeast nuclear pore targeting… · an experimental structure of the same protein · chain A against A, TM-score 0.12
- 2AIV · Multiple conformations in the ligand-binding site of the yeast nuclear pore targeting… · an experimental structure of the same protein · chain A against A, TM-score 0.12
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 Q02630
- Elsewhere: UniProt Q02630 · AlphaFold DB Q02630
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