Research workbench
AlphaFold monomer V2.0 prediction for arginine--tRNA ligase (C5D9R0)
Analyse AlphaFold monomer V2.0 prediction for arginine--tRNA ligase (C5D9R0) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- C5D9R0
- Type
- protein
- Length
- 556 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xB3Ab416696389A921046DDA22F83Be8e512fde4d
- Molecule
- Arginine--tRNA ligase
- UniProt
- C5D9R0
- Pockets
- 3 · best druggability 0.67
Structure
1 distinct chain · 55% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Arginine--tRNA ligase | protein | 556 | 55% helix, 14% strand | C5D9R0 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 451 | 0.67 | 0.79 | 49 | empty |
| 2 | 227 | 0.48 | 0.74 | 30 | empty |
| 3 | 117 | 0.35 | 0.73 | 23 | 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 C5D9R0
- Elsewhere: UniProt C5D9R0 · AlphaFold DB C5D9R0
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