Research workbench
AlphaFold monomer V2.0 prediction for arginine--tRNA ligase (B3DPJ1)
Analyse AlphaFold monomer V2.0 prediction for arginine--tRNA ligase (B3DPJ1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B3DPJ1
- Type
- protein
- Length
- 620 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x6154deB236274613b612033257012c25F7431808
- Molecule
- Arginine--tRNA ligase
- UniProt
- B3DPJ1
- Pockets
- 4 · best druggability 0.69
Structure
1 distinct chain · 52% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Arginine--tRNA ligase | protein | 620 | 52% helix, 13% strand | B3DPJ1 |
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 | 549 | 0.69 | 0.78 | 53 | empty |
| 2 | 119 | 0.47 | 0.79 | 23 | empty |
| 3 | 177 | 0.43 | 0.74 | 28 | empty |
| 4 | 83 | 0.37 | 0.77 | 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 B3DPJ1
- Elsewhere: UniProt B3DPJ1 · AlphaFold DB B3DPJ1
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