Research workbench
AlphaFold monomer V2.0 prediction for arginine--tRNA ligase (B7V3E4)
Analyse AlphaFold monomer V2.0 prediction for arginine--tRNA ligase (B7V3E4) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B7V3E4
- Type
- protein
- Length
- 587 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x299fdAcA3f0bf08962C6B6e8201Eb8953a8483fB
- Molecule
- Arginine--tRNA ligase
- UniProt
- B7V3E4
- Pockets
- 6 · best druggability 0.66
Structure
1 distinct chain · 56% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Arginine--tRNA ligase | protein | 587 | 56% helix, 12% strand | B7V3E4 |
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 432 | 0.66 | 0.78 | 51 | empty |
| 2 | 317 | 0.59 | 0.77 | 41 | empty |
| 3 | 87 | 0.44 | 0.80 | 17 | empty |
| 4 | 55 | 0.43 | 0.82 | 14 | empty |
| 5 | 113 | 0.42 | 0.77 | 18 | 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 B7V3E4
- Elsewhere: UniProt B7V3E4 · AlphaFold DB B7V3E4
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