Research workbench
AlphaFold monomer V2.0 prediction for cysteine--tRNA ligase (Q0AM03)
Analyse AlphaFold monomer V2.0 prediction for cysteine--tRNA ligase (Q0AM03) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q0AM03
- Type
- protein
- Length
- 461 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xA69277C1912f2C1a1dF13BfDFDd59c0e314Da1B7
- Molecule
- Cysteine--tRNA ligase
- UniProt
- Q0AM03
- Pockets
- 4 · best druggability 0.70
Structure
1 distinct chain · 49% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cysteine--tRNA ligase | protein | 461 | 49% helix, 17% strand | Q0AM03 |
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 | 347 | 0.70 | 0.83 | 44 | empty |
| 2 | 70 | 0.35 | 0.76 | 18 | empty |
| 3 | 59 | 0.31 | 0.76 | 13 | empty |
| 4 | 55 | 0.29 | 0.75 | 14 | 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 Q0AM03
- Elsewhere: UniProt Q0AM03 · AlphaFold DB Q0AM03
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