Research workbench
AlphaFold monomer V2.0 prediction for serine--tRNA ligase (A9L269)
Analyse AlphaFold monomer V2.0 prediction for serine--tRNA ligase (A9L269) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A9L269
- Type
- protein
- Length
- 428 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x3e8e3909a877B69b46206B47B350b98db3C5644b
- Molecule
- Serine--tRNA ligase
- UniProt
- A9L269
- Pockets
- 4 · best druggability 0.73
Structure
1 distinct chain · 44% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Serine--tRNA ligase | protein | 428 | 44% helix, 20% strand | A9L269 |
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 | 634 | 0.73 | 0.80 | 56 | empty |
| 2 | 77 | 0.42 | 0.79 | 17 | empty |
| 3 | 90 | 0.41 | 0.78 | 13 | empty |
| 4 | 69 | 0.34 | 0.76 | 12 | 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 A9L269
- Elsewhere: UniProt A9L269 · AlphaFold DB A9L269
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