Research workbench
AlphaFold monomer V2.0 prediction for cysteine--tRNA ligase (Q164A4)
Analyse AlphaFold monomer V2.0 prediction for cysteine--tRNA ligase (Q164A4) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q164A4
- Type
- protein
- Length
- 473 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x6Bba4Dfcacaa163872Cb467D38Fc0e76d3D00cF3
- Molecule
- Cysteine--tRNA ligase
- UniProt
- Q164A4
- Pockets
- 4 · best druggability 0.64
Structure
1 distinct chain · 49% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cysteine--tRNA ligase | protein | 473 | 49% helix, 18% strand | Q164A4 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 268 | 0.64 | 0.81 | 37 | empty |
| 2 | 363 | 0.56 | 0.74 | 35 | empty |
| 3 | 98 | 0.36 | 0.74 | 26 | empty |
| 4 | 79 | 0.31 | 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 Q164A4
- Elsewhere: UniProt Q164A4 · AlphaFold DB Q164A4
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