Research workbench
AlphaFold monomer V2.0 prediction for nuclear cap-binding protein subunit 2 (Q93594)
Analyse AlphaFold monomer V2.0 prediction for nuclear cap-binding protein subunit 2… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q93594
- Type
- protein
- Length
- 158 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5e58272ea25a05e06901A2eAe9f63939b344e0c6
- Molecule
- Nuclear cap-binding protein subunit 2
- UniProt
- Q93594
- Pockets
- 3 · best druggability 0.53
Structure
1 distinct chain · 30% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nuclear cap-binding protein subunit 2 | protein | 158 | 30% helix, 21% strand | Q93594 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 192 | 0.53 | 0.78 | 20 | empty |
| 2 | 121 | 0.46 | 0.79 | 20 | empty |
| 3 | 66 | 0.46 | 0.83 | 16 | 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 Q93594
- Elsewhere: UniProt Q93594 · AlphaFold DB Q93594
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