Research workbench
AlphaFold monomer V2.0 prediction for polypyrimidine tract-binding protein 1 (P17225)
Analyse AlphaFold monomer V2.0 prediction for polypyrimidine tract-binding protein 1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P17225
- Type
- protein
- Length
- 527 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xd91633319BDB0a92cbC4f08DeA734Bf74C030064
- Molecule
- Polypyrimidine tract-binding protein 1
- UniProt
- P17225
- Pockets
- 6 · best druggability 0.64
Structure
1 distinct chain · 19% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Polypyrimidine tract-binding protein 1 | protein | 527 | 19% helix, 20% strand | P17225 |
Pockets
6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 187 | 0.64 | 0.84 | 30 | empty |
| 2 | 352 | 0.63 | 0.78 | 35 | empty |
| 3 | 412 | 0.56 | 0.74 | 46 | empty |
| 4 | 239 | 0.50 | 0.75 | 27 | empty |
| 5 | 68 | 0.29 | 0.73 | 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 P17225
- Elsewhere: UniProt P17225 · AlphaFold DB P17225
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