Research workbench
AlphaFold monomer V2.0 prediction for protein adenylyltransferase selo (A9IT50)
Analyse AlphaFold monomer V2.0 prediction for protein adenylyltransferase selo (A9IT50) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A9IT50
- Type
- protein
- Length
- 497 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xB765e36a52DF056e3d74166883b608B9e6599Dd2
- Molecule
- Protein adenylyltransferase selo
- UniProt
- A9IT50
- Pockets
- 5 · best druggability 0.70
Structure
1 distinct chain · 47% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein adenylyltransferase selo | protein | 497 | 47% helix, 15% strand | A9IT50 |
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 434 | 0.70 | 0.82 | 51 | empty |
| 2 | 144 | 0.44 | 0.76 | 20 | empty |
| 3 | 74 | 0.38 | 0.78 | 16 | empty |
| 4 | 70 | 0.32 | 0.74 | 14 | empty |
| 5 | 59 | 0.28 | 0.73 | 13 | 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 A9IT50
- Elsewhere: UniProt A9IT50 · AlphaFold DB A9IT50
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