Research workbench
AlphaFold monomer V2.0 prediction for glutamate--tRNA ligase (A9BE95)
Analyse AlphaFold monomer V2.0 prediction for glutamate--tRNA ligase (A9BE95) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A9BE95
- Type
- protein
- Length
- 476 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9813De3d6CFC7786eA653839E1f43339E301FD92
- Molecule
- Glutamate--tRNA ligase
- UniProt
- A9BE95
- Pockets
- 4 · best druggability 0.66
Structure
1 distinct chain · 52% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutamate--tRNA ligase | protein | 476 | 52% helix, 13% strand | A9BE95 |
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 | 355 | 0.66 | 0.80 | 32 | empty |
| 2 | 123 | 0.41 | 0.75 | 17 | empty |
| 3 | 110 | 0.38 | 0.75 | 22 | empty |
| 4 | 70 | 0.33 | 0.75 | 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 A9BE95
- Elsewhere: UniProt A9BE95 · AlphaFold DB A9BE95
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