Research workbench
AlphaFold monomer V2.0 prediction for cysteine--tRNA ligase (A0KYM2)
Analyse AlphaFold monomer V2.0 prediction for cysteine--tRNA ligase (A0KYM2) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A0KYM2
- Type
- protein
- Length
- 461 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x520AB67aC243f53328F015981f71b4911C1030B0
- Molecule
- Cysteine--tRNA ligase
- UniProt
- A0KYM2
- Pockets
- 4 · best druggability 0.70
Structure
1 distinct chain · 48% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cysteine--tRNA ligase | protein | 461 | 48% helix, 17% strand | A0KYM2 |
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 | 266 | 0.70 | 0.85 | 34 | empty |
| 2 | 107 | 0.36 | 0.74 | 23 | empty |
| 3 | 90 | 0.31 | 0.73 | 18 | empty |
| 4 | 50 | 0.27 | 0.74 | 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 A0KYM2
- Elsewhere: UniProt A0KYM2 · AlphaFold DB A0KYM2
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