Research workbench
AlphaFold monomer V2.0 prediction for nuclear cap-binding protein subunit 2 (Q177H0)
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
- Q177H0
- Type
- protein
- Length
- 159 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xEF5B88e5Ca3A2EcE562c6102eF428a1bBAB32b9e
- Molecule
- Nuclear cap-binding protein subunit 2
- UniProt
- Q177H0
- Pockets
- 1 · best druggability 0.50
Structure
1 distinct chain · 27% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nuclear cap-binding protein subunit 2 | protein | 159 | 27% helix, 21% strand | Q177H0 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 151 | 0.50 | 0.79 | 22 | 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 Q177H0
- Elsewhere: UniProt Q177H0 · AlphaFold DB Q177H0
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