Research workbench
AlphaFold monomer V2.0 prediction for glutamate--tRNA ligase (A1VBA3)
Analyse AlphaFold monomer V2.0 prediction for glutamate--tRNA ligase (A1VBA3) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A1VBA3
- Type
- protein
- Length
- 463 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x3298b100681D3A2372Bba3b2f282750dD71629B9
- Molecule
- Glutamate--tRNA ligase
- UniProt
- A1VBA3
- Pockets
- 4 · best druggability 0.65
Structure
1 distinct chain · 52% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutamate--tRNA ligase | protein | 463 | 52% helix, 12% strand | A1VBA3 |
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 | 378 | 0.65 | 0.79 | 46 | empty |
| 2 | 127 | 0.41 | 0.75 | 18 | empty |
| 3 | 71 | 0.36 | 0.76 | 13 | empty |
| 4 | 91 | 0.31 | 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 A1VBA3
- Elsewhere: UniProt A1VBA3 · AlphaFold DB A1VBA3
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