Research workbench
AlphaFold monomer V2.0 prediction for tyrosine--tRNA ligase (Q5XE99)
Analyse AlphaFold monomer V2.0 prediction for tyrosine--tRNA ligase (Q5XE99) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q5XE99
- Type
- protein
- Length
- 418 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x80D2ac0F5e3268bC5C1d28BBAA07E3169BB02b79
- Molecule
- Tyrosine--tRNA ligase
- UniProt
- Q5XE99
- Pockets
- 4 · best druggability 0.75
Structure
1 distinct chain · 50% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tyrosine--tRNA ligase | protein | 418 | 50% helix, 15% strand | Q5XE99 |
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 | 380 | 0.75 | 0.86 | 45 | empty |
| 2 | 222 | 0.46 | 0.73 | 32 | empty |
| 3 | 123 | 0.42 | 0.75 | 23 | empty |
| 4 | 80 | 0.40 | 0.78 | 15 | 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 Q5XE99
- Elsewhere: UniProt Q5XE99 · AlphaFold DB Q5XE99
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