Research workbench
AlphaFold monomer V2.0 prediction for nuclear pore complex protein NUP93 (A5PJZ5)
Analyse AlphaFold monomer V2.0 prediction for nuclear pore complex protein NUP93… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A5PJZ5
- Type
- protein
- Length
- 819 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x0EA189b2343A464f560b44103f6A3396Da1dA8a9
- Molecule
- Nuclear pore complex protein NUP93
- UniProt
- A5PJZ5
- Pockets
- 8 · best druggability 0.64
Structure
1 distinct chain · 65% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nuclear pore complex protein NUP93 | protein | 819 | 65% helix, 2% strand | A5PJZ5 |
Pockets
8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 597 | 0.64 | 0.75 | 45 | empty |
| 2 | 57 | 0.62 | 0.93 | 19 | empty |
| 3 | 100 | 0.54 | 0.84 | 18 | empty |
| 4 | 204 | 0.48 | 0.75 | 24 | empty |
| 5 | 134 | 0.48 | 0.78 | 24 | 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 A5PJZ5
- Elsewhere: UniProt A5PJZ5 · AlphaFold DB A5PJZ5
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