Research workbench
AlphaFold monomer V2.0 prediction for tyrosine--tRNA ligase (B2VEN3)
Analyse AlphaFold monomer V2.0 prediction for tyrosine--tRNA ligase (B2VEN3) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B2VEN3
- Type
- protein
- Length
- 425 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xbb2F1C7CB3A1eeFAc24fCa72cc627162D5413FD7
- Molecule
- Tyrosine--tRNA ligase
- UniProt
- B2VEN3
- Pockets
- 4 · best druggability 0.71
Structure
1 distinct chain · 49% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tyrosine--tRNA ligase | protein | 425 | 49% helix, 16% strand | B2VEN3 |
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 | 415 | 0.71 | 0.82 | 47 | empty |
| 2 | 90 | 0.37 | 0.75 | 15 | empty |
| 3 | 88 | 0.34 | 0.74 | 20 | empty |
| 4 | 67 | 0.33 | 0.76 | 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 B2VEN3
- Elsewhere: UniProt B2VEN3 · AlphaFold DB B2VEN3
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