Research workbench
AlphaFold monomer V2.0 prediction for retrovirus-related pol polyprotein from transposon 412 (P10394)
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
- P10394
- Type
- protein
- Length
- 1,237 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x38EB5C873A97281Ed18Da8DA93921002c6195C4D
- Molecule
- Retrovirus-related pol polyprotein from transposon 412
- UniProt
- P10394
- Pockets
- 17 · best druggability 0.79
Structure
1 distinct chain · 34% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Retrovirus-related pol polyprotein from transposon 412 | protein | 1237 | 34% helix, 24% strand | P10394 |
Pockets
17 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1147 | 0.79 | 0.81 | 83 | empty |
| 2 | 786 | 0.72 | 0.78 | 68 | empty |
| 3 | 479 | 0.67 | 0.78 | 46 | empty |
| 4 | 381 | 0.64 | 0.78 | 32 | empty |
| 5 | 103 | 0.54 | 0.84 | 23 | 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 P10394
- Elsewhere: UniProt P10394 · AlphaFold DB P10394
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