Research workbench
AlphaFold monomer V2.0 prediction for nuclear cap-binding protein subunit 1 (B4Q034)
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
- B4Q034
- Type
- protein
- Length
- 800 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x91A3Ff8006565B92Be90f7924A65De16701cc9fb
- Molecule
- Nuclear cap-binding protein subunit 1
- UniProt
- B4Q034
- Pockets
- 12 · best druggability 0.74
Structure
1 distinct chain · 67% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nuclear cap-binding protein subunit 1 | protein | 800 | 67% helix, 1% strand | B4Q034 |
Pockets
12 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 451 | 0.74 | 0.83 | 45 | empty |
| 2 | 315 | 0.68 | 0.82 | 36 | empty |
| 3 | 277 | 0.64 | 0.81 | 25 | empty |
| 4 | 349 | 0.58 | 0.76 | 37 | empty |
| 5 | 136 | 0.47 | 0.77 | 17 | 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 B4Q034
- Elsewhere: UniProt B4Q034 · AlphaFold DB B4Q034
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