Research workbench
AlphaFold monomer V2.0 prediction for phenylalanine--tRNA ligase beta subunit (Q0SMZ4)
Analyse AlphaFold monomer V2.0 prediction for phenylalanine--tRNA ligase beta subunit… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q0SMZ4
- Type
- protein
- Length
- 567 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xe224E0Ef7bE7cF7f0C1043dd5Ab8882d57b81d32
- Molecule
- Phenylalanine--tRNA ligase beta subunit
- UniProt
- Q0SMZ4
- Pockets
- 3 · best druggability 0.60
Structure
1 distinct chain · 33% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phenylalanine--tRNA ligase beta subunit | protein | 567 | 33% helix, 28% strand | Q0SMZ4 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 328 | 0.60 | 0.77 | 29 | empty |
| 2 | 161 | 0.56 | 0.81 | 27 | empty |
| 3 | 56 | 0.39 | 0.80 | 17 | 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 Q0SMZ4
- Elsewhere: UniProt Q0SMZ4 · AlphaFold DB Q0SMZ4
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