Research workbench
AlphaFold monomer V2.0 prediction for nuclear cap-binding protein subunit 1 (Q29G82)
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
- Q29G82
- Type
- protein
- Length
- 800 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x97EfFf2d74994e28D3b69b1503Bd9c292B2Df480
- Molecule
- Nuclear cap-binding protein subunit 1
- UniProt
- Q29G82
- Pockets
- 9 · best druggability 0.75
Structure
1 distinct chain · 67% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nuclear cap-binding protein subunit 1 | protein | 800 | 67% helix, 1% strand | Q29G82 |
Pockets
9 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 489 | 0.75 | 0.83 | 52 | empty |
| 2 | 326 | 0.67 | 0.81 | 37 | empty |
| 3 | 274 | 0.62 | 0.80 | 26 | empty |
| 4 | 321 | 0.56 | 0.75 | 33 | empty |
| 5 | 122 | 0.43 | 0.77 | 18 | 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 Q29G82
- Elsewhere: UniProt Q29G82 · AlphaFold DB Q29G82
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.