Research workbench
AlphaFold monomer V2.0 prediction for nuclear cap-binding protein subunit 1 (B4GW22)
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
- B4GW22
- Type
- protein
- Length
- 800 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x4925F35C539c838F29Bff8dbDd7f50009BD3f044
- Molecule
- Nuclear cap-binding protein subunit 1
- UniProt
- B4GW22
- Pockets
- 11 · best druggability 0.72
Structure
1 distinct chain · 66% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nuclear cap-binding protein subunit 1 | protein | 800 | 66% helix, 1% strand | B4GW22 |
Pockets
11 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 398 | 0.72 | 0.83 | 43 | empty |
| 2 | 314 | 0.67 | 0.81 | 34 | empty |
| 3 | 290 | 0.62 | 0.80 | 25 | empty |
| 4 | 352 | 0.57 | 0.75 | 37 | empty |
| 5 | 99 | 0.42 | 0.77 | 14 | 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 B4GW22
- Elsewhere: UniProt B4GW22 · AlphaFold DB B4GW22
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