Research workbench
AlphaFold monomer V2.0 prediction for arginine--tRNA ligase (B5EEF0)
Analyse AlphaFold monomer V2.0 prediction for arginine--tRNA ligase (B5EEF0) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B5EEF0
- Type
- protein
- Length
- 554 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xB44F19a0cb161828322eEEd13F55d4C3C34938d2
- Molecule
- Arginine--tRNA ligase
- UniProt
- B5EEF0
- Pockets
- 4 · best druggability 0.66
Structure
1 distinct chain · 54% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Arginine--tRNA ligase | protein | 554 | 54% helix, 13% strand | B5EEF0 |
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 | 468 | 0.66 | 0.78 | 50 | empty |
| 2 | 212 | 0.50 | 0.76 | 30 | empty |
| 3 | 82 | 0.34 | 0.74 | 14 | empty |
| 4 | 51 | 0.28 | 0.75 | 20 | 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 B5EEF0
- Elsewhere: UniProt B5EEF0 · AlphaFold DB B5EEF0
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