Research workbench
AlphaFold monomer V2.0 prediction for nuclear cap-binding protein subunit 1 (Q55D17)
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
- Q55D17
- Type
- protein
- Length
- 772 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xf87a97E0A4bB354D834857B14296240B167cbe70
- Molecule
- Nuclear cap-binding protein subunit 1
- UniProt
- Q55D17
- Pockets
- 11 · 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 | 772 | 67% helix, 1% strand | Q55D17 |
Pockets
11 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 84 | 0.75 | 0.98 | 24 | empty |
| 2 | 601 | 0.69 | 0.78 | 57 | empty |
| 3 | 337 | 0.60 | 0.78 | 47 | empty |
| 4 | 99 | 0.49 | 0.81 | 17 | empty |
| 5 | 173 | 0.47 | 0.76 | 25 | 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 Q55D17
- Elsewhere: UniProt Q55D17 · AlphaFold DB Q55D17
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