Research workbench
AlphaFold monomer V2.0 prediction for serine--tRNA ligase (Q8D265)
Analyse AlphaFold monomer V2.0 prediction for serine--tRNA ligase (Q8D265) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q8D265
- Type
- protein
- Length
- 429 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7FDF8b382C6a36A8772D1A265E8e480c7DF0A9C1
- Molecule
- Serine--tRNA ligase
- UniProt
- Q8D265
- Pockets
- 3 · best druggability 0.73
Structure
1 distinct chain · 44% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Serine--tRNA ligase | protein | 429 | 44% helix, 21% strand | Q8D265 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 645 | 0.73 | 0.80 | 52 | empty |
| 2 | 98 | 0.39 | 0.76 | 22 | empty |
| 3 | 58 | 0.30 | 0.75 | 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 Q8D265
- Elsewhere: UniProt Q8D265 · AlphaFold DB Q8D265
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