Research workbench
AlphaFold monomer V2.0 prediction for cysteine--tRNA ligase (A9N924)
Analyse AlphaFold monomer V2.0 prediction for cysteine--tRNA ligase (A9N924) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A9N924
- Type
- protein
- Length
- 458 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x4d07E6a23DeB6B95bd9b90EcB67368b7e8D3B77e
- Molecule
- Cysteine--tRNA ligase
- UniProt
- A9N924
- Pockets
- 3 · best druggability 0.67
Structure
1 distinct chain · 48% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cysteine--tRNA ligase | protein | 458 | 48% helix, 18% strand | A9N924 |
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 | 312 | 0.67 | 0.82 | 37 | empty |
| 2 | 154 | 0.48 | 0.77 | 20 | empty |
| 3 | 184 | 0.46 | 0.75 | 26 | 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 A9N924
- Elsewhere: UniProt A9N924 · AlphaFold DB A9N924
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