Research workbench
AlphaFold monomer V2.0 prediction for nuclear cap-binding protein subunit 1-B (Q6GQD0)
Analyse AlphaFold monomer V2.0 prediction for nuclear cap-binding protein subunit 1-B… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q6GQD0
- Type
- protein
- Length
- 791 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xF25799609c3112487CBaCFd8059A5b2D59a35379
- Molecule
- Nuclear cap-binding protein subunit 1-B
- UniProt
- Q6GQD0
- Pockets
- 12 · best druggability 0.75
Structure
1 distinct chain · 68% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nuclear cap-binding protein subunit 1-B | protein | 791 | 68% helix, 1% strand | Q6GQD0 |
Pockets
12 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 479 | 0.75 | 0.84 | 50 | empty |
| 2 | 224 | 0.62 | 0.82 | 27 | empty |
| 3 | 59 | 0.58 | 0.91 | 21 | empty |
| 4 | 312 | 0.57 | 0.76 | 40 | empty |
| 5 | 106 | 0.43 | 0.78 | 29 | 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 Q6GQD0
- Elsewhere: UniProt Q6GQD0 · AlphaFold DB Q6GQD0
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.