Research workbench
AlphaFold monomer V2.0 prediction for transposon TY1-ER2 gag polyprotein (P0CX66)
Analyse AlphaFold monomer V2.0 prediction for transposon TY1-ER2 gag polyprotein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P0CX66
- Type
- protein
- Length
- 440 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x661f92Fc5950020C7aB410B5F5b9a3f429F49Ae5
- Molecule
- Transposon TY1-ER2 gag polyprotein
- UniProt
- P0CX66
- Pockets
- 3 · best druggability 0.45
Structure
1 distinct chain · 31% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transposon TY1-ER2 gag polyprotein | protein | 440 | 31% helix, 0% strand | P0CX66 |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 218 | 0.45 | 0.73 | 20 | empty |
| 2 | 51 | 0.33 | 0.78 | 12 | empty |
| 3 | 53 | 0.30 | 0.76 | 14 | 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 P0CX66
- Elsewhere: UniProt P0CX66 · AlphaFold DB P0CX66
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