Research workbench
AlphaFold monomer V2.0 prediction for nuclear cap-binding protein subunit 1 (O14253)
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
- O14253
- Type
- protein
- Length
- 780 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5Ed6b66622087Dc1983A2090Bc20a6F5E42E57c1
- Molecule
- Nuclear cap-binding protein subunit 1
- UniProt
- O14253
- Pockets
- 7 · best druggability 0.69
Structure
1 distinct chain · 62% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nuclear cap-binding protein subunit 1 | protein | 780 | 62% helix, 1% strand | O14253 |
Pockets
7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 311 | 0.69 | 0.83 | 36 | empty |
| 2 | 419 | 0.58 | 0.74 | 46 | empty |
| 3 | 237 | 0.55 | 0.77 | 32 | empty |
| 4 | 160 | 0.55 | 0.81 | 26 | empty |
| 5 | 251 | 0.48 | 0.74 | 28 | 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 O14253
- Elsewhere: UniProt O14253 · AlphaFold DB O14253
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