Research workbench
AlphaFold monomer V2.0 prediction for nuclear cap-binding protein subunit 2 (Q84L14)
Analyse AlphaFold monomer V2.0 prediction for nuclear cap-binding protein subunit 2… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q84L14
- Type
- protein
- Length
- 243 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x4d07E6a23DeB6B95bd9b90EcB67368b7e8D3B77e
- Molecule
- Nuclear cap-binding protein subunit 2
- UniProt
- Q84L14
- Pockets
- 3 · best druggability 0.52
Structure
1 distinct chain · 22% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nuclear cap-binding protein subunit 2 | protein | 243 | 22% helix, 14% strand | Q84L14 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 150 | 0.52 | 0.80 | 20 | empty |
| 2 | 67 | 0.35 | 0.78 | 22 | empty |
| 3 | 51 | 0.33 | 0.78 | 14 | 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 Q84L14
- Elsewhere: UniProt Q84L14 · AlphaFold DB Q84L14
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