Research workbench
AlphaFold monomer V2.0 prediction for protein adenylyltransferase selo (Q12AE5)
Analyse AlphaFold monomer V2.0 prediction for protein adenylyltransferase selo (Q12AE5) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q12AE5
- Type
- protein
- Length
- 496 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xc82F9335615A608209Fb2E5283c0EcA331b85A66
- Molecule
- Protein adenylyltransferase selo
- UniProt
- Q12AE5
- Pockets
- 6 · best druggability 0.67
Structure
1 distinct chain · 46% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein adenylyltransferase selo | protein | 496 | 46% helix, 15% strand | Q12AE5 |
Pockets
6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 321 | 0.67 | 0.82 | 38 | empty |
| 2 | 185 | 0.48 | 0.75 | 16 | empty |
| 3 | 54 | 0.42 | 0.82 | 11 | empty |
| 4 | 92 | 0.41 | 0.78 | 21 | empty |
| 5 | 103 | 0.37 | 0.75 | 25 | 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 Q12AE5
- Elsewhere: UniProt Q12AE5 · AlphaFold DB Q12AE5
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