Research workbench
AlphaFold monomer V2.0 prediction for nuclear cap-binding protein subunit 3 (Q53F19)
Analyse AlphaFold monomer V2.0 prediction for nuclear cap-binding protein subunit 3… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q53F19
- Type
- protein
- Length
- 620 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x0C565B44183A2EdEAd47c93586302667F007a919
- Molecule
- Nuclear cap-binding protein subunit 3
- UniProt
- Q53F19
- Pockets
- 3 · best druggability 0.70
Structure
1 distinct chain · 29% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nuclear cap-binding protein subunit 3 | protein | 620 | 29% helix, 5% strand | Q53F19 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 371 | 0.70 | 0.82 | 50 | empty |
| 2 | 308 | 0.53 | 0.75 | 39 | empty |
| 3 | 216 | 0.49 | 0.75 | 29 | empty |
Compared structures
- 8BY6 · Structure of the human nuclear cap-binding complex bound to NCBP3(560-620) and… · an experimental structure of the same protein · chain A against C, TM-score 0.04
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 Q53F19
- Elsewhere: UniProt Q53F19 · AlphaFold DB Q53F19
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.