Research workbench
AlphaFold monomer V2.0 prediction for tyrosine--tRNA ligase (A5FMI1)
Analyse AlphaFold monomer V2.0 prediction for tyrosine--tRNA ligase (A5FMI1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A5FMI1
- Type
- protein
- Length
- 431 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xd91633319BDB0a92cbC4f08DeA734Bf74C030064
- Molecule
- Tyrosine--tRNA ligase
- UniProt
- A5FMI1
- Pockets
- 3 · best druggability 0.76
Structure
1 distinct chain · 50% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tyrosine--tRNA ligase | protein | 431 | 50% helix, 15% strand | A5FMI1 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 568 | 0.76 | 0.83 | 49 | empty |
| 2 | 122 | 0.40 | 0.74 | 22 | empty |
| 3 | 124 | 0.39 | 0.74 | 30 | 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 A5FMI1
- Elsewhere: UniProt A5FMI1 · AlphaFold DB A5FMI1
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