Research workbench
AlphaFold monomer V2.0 prediction for protein adenylyltransferase selo (Q164E9)
Analyse AlphaFold monomer V2.0 prediction for protein adenylyltransferase selo (Q164E9) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q164E9
- Type
- protein
- Length
- 470 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7F60C0720a0abd27E21935aE2E36C4d984db2FEC
- Molecule
- Protein adenylyltransferase selo
- UniProt
- Q164E9
- Pockets
- 4 · best druggability 0.73
Structure
1 distinct chain · 46% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein adenylyltransferase selo | protein | 470 | 46% helix, 16% strand | Q164E9 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 467 | 0.73 | 0.82 | 57 | empty |
| 2 | 132 | 0.39 | 0.73 | 18 | empty |
| 3 | 75 | 0.35 | 0.76 | 19 | empty |
| 4 | 80 | 0.33 | 0.75 | 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 Q164E9
- Elsewhere: UniProt Q164E9 · AlphaFold DB Q164E9
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