Research workbench
AlphaFold monomer V2.0 prediction for arginine--tRNA ligase (Q9CE12)
Analyse AlphaFold monomer V2.0 prediction for arginine--tRNA ligase (Q9CE12) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9CE12
- Type
- protein
- Length
- 564 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x362a6d063b1B7E1B6EfD3A9A7CA3612e3FE037AA
- Molecule
- Arginine--tRNA ligase
- UniProt
- Q9CE12
- Pockets
- 5 · best druggability 0.66
Structure
1 distinct chain · 60% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Arginine--tRNA ligase | protein | 564 | 60% helix, 11% strand | Q9CE12 |
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 466 | 0.66 | 0.78 | 46 | empty |
| 2 | 246 | 0.55 | 0.77 | 35 | empty |
| 3 | 91 | 0.34 | 0.74 | 17 | empty |
| 4 | 50 | 0.26 | 0.74 | 13 | empty |
| 5 | 56 | 0.26 | 0.72 | 16 | 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 Q9CE12
- Elsewhere: UniProt Q9CE12 · AlphaFold DB Q9CE12
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