Research workbench
AlphaFold monomer V2.0 prediction for tyrosine--tRNA ligase (B3CM50)
Analyse AlphaFold monomer V2.0 prediction for tyrosine--tRNA ligase (B3CM50) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B3CM50
- Type
- protein
- Length
- 420 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xb3c0C983Fc44934AC589D7131C08a72544EBB92E
- Molecule
- Tyrosine--tRNA ligase
- UniProt
- B3CM50
- Pockets
- 4 · best druggability 0.76
Structure
1 distinct chain · 49% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tyrosine--tRNA ligase | protein | 420 | 49% helix, 15% strand | B3CM50 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 422 | 0.76 | 0.85 | 46 | empty |
| 2 | 366 | 0.60 | 0.76 | 41 | empty |
| 3 | 78 | 0.34 | 0.76 | 18 | empty |
| 4 | 65 | 0.34 | 0.76 | 14 | 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 B3CM50
- Elsewhere: UniProt B3CM50 · AlphaFold DB B3CM50
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