Research workbench
AlphaFold monomer V2.0 prediction for polyadenylate-binding protein, cytoplasmic and nuclear (A5DW14)
Analyse AlphaFold monomer V2.0 prediction for polyadenylate-binding protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A5DW14
- Type
- protein
- Length
- 661 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x4d07E6a23DeB6B95bd9b90EcB67368b7e8D3B77e
- Molecule
- Polyadenylate-binding protein, cytoplasmic and nuclear
- UniProt
- A5DW14
- Pockets
- 6 · best druggability 0.55
Structure
1 distinct chain · 37% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Polyadenylate-binding protein, cytoplasmic and nuclear | protein | 661 | 37% helix, 18% strand | A5DW14 |
Pockets
6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 315 | 0.55 | 0.75 | 26 | empty |
| 2 | 114 | 0.41 | 0.76 | 26 | empty |
| 3 | 128 | 0.37 | 0.73 | 19 | empty |
| 4 | 81 | 0.37 | 0.76 | 16 | empty |
| 5 | 75 | 0.32 | 0.74 | 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 A5DW14
- Elsewhere: UniProt A5DW14 · AlphaFold DB A5DW14
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