Research workbench
AlphaFold monomer V2.0 prediction for polyadenylate-binding protein 1A (F1QB54)
Analyse AlphaFold monomer V2.0 prediction for polyadenylate-binding protein 1A (F1QB54) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- F1QB54
- Type
- protein
- Length
- 634 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xB44F19a0cb161828322eEEd13F55d4C3C34938d2
- Molecule
- Polyadenylate-binding protein 1A
- UniProt
- F1QB54
- Pockets
- 4 · best druggability 0.60
Structure
1 distinct chain · 34% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Polyadenylate-binding protein 1A | protein | 634 | 34% helix, 20% strand | F1QB54 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 484 | 0.60 | 0.75 | 47 | empty |
| 2 | 318 | 0.57 | 0.76 | 41 | empty |
| 3 | 128 | 0.39 | 0.74 | 19 | empty |
| 4 | 56 | 0.28 | 0.74 | 10 | 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 F1QB54
- Elsewhere: UniProt F1QB54 · AlphaFold DB F1QB54
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