Research workbench
AlphaFold monomer V2.0 prediction for nuclear cap-binding protein subunit 2 (A8Y1R8)
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
- A8Y1R8
- Type
- protein
- Length
- 157 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x203931C4dCE9665F4d5cF5934d3Ae3C09C32cf88
- Molecule
- Nuclear cap-binding protein subunit 2
- UniProt
- A8Y1R8
- Pockets
- 3 · best druggability 0.52
Structure
1 distinct chain · 29% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nuclear cap-binding protein subunit 2 | protein | 157 | 29% helix, 21% strand | A8Y1R8 |
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 | 171 | 0.52 | 0.78 | 20 | empty |
| 2 | 94 | 0.49 | 0.82 | 20 | empty |
| 3 | 52 | 0.34 | 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 A8Y1R8
- Elsewhere: UniProt A8Y1R8 · AlphaFold DB A8Y1R8
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.