Research workbench
AlphaFold monomer V2.0 prediction for glutamate--tRNA ligase (A5UG92)
Analyse AlphaFold monomer V2.0 prediction for glutamate--tRNA ligase (A5UG92) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A5UG92
- Type
- protein
- Length
- 480 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x6227512B0B04f05c48A3f9Bb2A26C737dAb650E8
- Molecule
- Glutamate--tRNA ligase
- UniProt
- A5UG92
- Pockets
- 4 · best druggability 0.67
Structure
1 distinct chain · 52% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutamate--tRNA ligase | protein | 480 | 52% helix, 12% strand | A5UG92 |
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 | 303 | 0.67 | 0.82 | 35 | empty |
| 2 | 102 | 0.35 | 0.74 | 16 | empty |
| 3 | 66 | 0.34 | 0.76 | 24 | empty |
| 4 | 81 | 0.32 | 0.74 | 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 A5UG92
- Elsewhere: UniProt A5UG92 · AlphaFold DB A5UG92
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