Research workbench
AlphaFold monomer V2.0 prediction for polyadenylate-binding protein 1-a (P20965)
Analyse AlphaFold monomer V2.0 prediction for polyadenylate-binding protein 1-a (P20965) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P20965
- Type
- protein
- Length
- 633 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9188600a0FCa2914254C94299b1bd9721Bc4D500
- Molecule
- Polyadenylate-binding protein 1-a
- UniProt
- P20965
- Pockets
- 5 · best druggability 0.61
Structure
1 distinct chain · 34% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Polyadenylate-binding protein 1-a | protein | 633 | 34% helix, 20% strand | P20965 |
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 498 | 0.61 | 0.75 | 46 | empty |
| 2 | 256 | 0.53 | 0.76 | 27 | empty |
| 3 | 69 | 0.35 | 0.77 | 21 | empty |
| 4 | 90 | 0.33 | 0.74 | 19 | empty |
| 5 | 50 | 0.33 | 0.78 | 12 | 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 P20965
- Elsewhere: UniProt P20965 · AlphaFold DB P20965
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