Research workbench
AlphaFold monomer V2.0 prediction for nuclear cap-binding protein subunit 1 (Q10LJ0)
Analyse AlphaFold monomer V2.0 prediction for nuclear cap-binding protein subunit 1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q10LJ0
- Type
- protein
- Length
- 867 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xdF2b063d4B94F3f46D117B1af99A846bD4a59284
- Molecule
- Nuclear cap-binding protein subunit 1
- UniProt
- Q10LJ0
- Pockets
- 10 · best druggability 0.83
Structure
1 distinct chain · 66% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nuclear cap-binding protein subunit 1 | protein | 867 | 66% helix, 1% strand | Q10LJ0 |
Pockets
10 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1078 | 0.83 | 0.84 | 105 | empty |
| 2 | 74 | 0.75 | 0.99 | 22 | empty |
| 3 | 324 | 0.51 | 0.73 | 31 | empty |
| 4 | 197 | 0.50 | 0.77 | 33 | empty |
| 5 | 87 | 0.46 | 0.81 | 22 | 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 Q10LJ0
- Elsewhere: UniProt Q10LJ0 · AlphaFold DB Q10LJ0
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