Research workbench
AlphaFold monomer V2.0 prediction for cysteine--tRNA ligase (A2RMS1)
Analyse AlphaFold monomer V2.0 prediction for cysteine--tRNA ligase (A2RMS1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A2RMS1
- Type
- protein
- Length
- 448 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x01970A7586aE074a277adA45533563056BA700c1
- Molecule
- Cysteine--tRNA ligase
- UniProt
- A2RMS1
- Pockets
- 4 · best druggability 0.71
Structure
1 distinct chain · 49% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cysteine--tRNA ligase | protein | 448 | 49% helix, 19% strand | A2RMS1 |
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 | 534 | 0.71 | 0.80 | 75 | empty |
| 2 | 147 | 0.42 | 0.75 | 28 | empty |
| 3 | 67 | 0.32 | 0.75 | 16 | empty |
| 4 | 54 | 0.30 | 0.76 | 9 | 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 A2RMS1
- Elsewhere: UniProt A2RMS1 · AlphaFold DB A2RMS1
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