Research workbench
AlphaFold monomer V2.0 prediction for arginine--tRNA ligase (Q9PGZ9)
Analyse AlphaFold monomer V2.0 prediction for arginine--tRNA ligase (Q9PGZ9) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9PGZ9
- Type
- protein
- Length
- 562 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7a1388B6Aad67B04634A32f63b8A6D6005eab86c
- Molecule
- Arginine--tRNA ligase
- UniProt
- Q9PGZ9
- Pockets
- 4 · best druggability 0.68
Structure
1 distinct chain · 51% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Arginine--tRNA ligase | protein | 562 | 51% helix, 14% strand | Q9PGZ9 |
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 | 516 | 0.68 | 0.78 | 60 | empty |
| 2 | 160 | 0.43 | 0.74 | 29 | empty |
| 3 | 65 | 0.33 | 0.76 | 12 | empty |
| 4 | 77 | 0.31 | 0.73 | 15 | 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 Q9PGZ9
- Elsewhere: UniProt Q9PGZ9 · AlphaFold DB Q9PGZ9
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