Research workbench
AlphaFold monomer V2.0 prediction for cysteine--tRNA ligase (C6BS23)
Analyse AlphaFold monomer V2.0 prediction for cysteine--tRNA ligase (C6BS23) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- C6BS23
- Type
- protein
- Length
- 485 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xBeB220F0B5b0C48F46B5DDd3E3b071BC0827f8D6
- Molecule
- Cysteine--tRNA ligase
- UniProt
- C6BS23
- Pockets
- 4 · best druggability 0.66
Structure
1 distinct chain · 51% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cysteine--tRNA ligase | protein | 485 | 51% helix, 18% strand | C6BS23 |
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 | 317 | 0.66 | 0.81 | 41 | empty |
| 2 | 175 | 0.45 | 0.75 | 28 | empty |
| 3 | 134 | 0.41 | 0.75 | 18 | empty |
| 4 | 54 | 0.29 | 0.75 | 11 | 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 C6BS23
- Elsewhere: UniProt C6BS23 · AlphaFold DB C6BS23
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