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AlphaFold monomer V2.0 prediction for retrovirus-related pol polyprotein from type-1 retrotransposable element R1 (Q03276)
Analyse AlphaFold monomer V2.0 prediction for retrovirus-related pol polyprotein from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q03276
- Type
- protein
- Length
- 245 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5e58272ea25a05e06901A2eAe9f63939b344e0c6
- Molecule
- Retrovirus-related pol polyprotein from type-1 retrotransposable element R1
- UniProt
- Q03276
- Pockets
- 3 · best druggability 0.50
Structure
1 distinct chain · 58% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Retrovirus-related pol polyprotein from type-1 retrotransposable element R1 | protein | 245 | 58% helix, 5% strand | Q03276 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 306 | 0.50 | 0.73 | 39 | empty |
| 2 | 119 | 0.43 | 0.76 | 16 | empty |
| 3 | 66 | 0.35 | 0.77 | 18 | 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 Q03276
- Elsewhere: UniProt Q03276 · AlphaFold DB Q03276
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