Research workbench
AlphaFold monomer V2.0 prediction for tyrosine--tRNA ligase (P83453)
Analyse AlphaFold monomer V2.0 prediction for tyrosine--tRNA ligase (P83453) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P83453
- Type
- protein
- Length
- 432 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xc663c339B33EBB31b84039575e218358B8FeD238
- Molecule
- Tyrosine--tRNA ligase
- UniProt
- P83453
- Pockets
- 5 · best druggability 0.83
Structure
1 distinct chain · 47% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tyrosine--tRNA ligase | protein | 432 | 47% helix, 14% strand | P83453 |
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 430 | 0.83 | 0.91 | 49 | empty |
| 2 | 69 | 0.43 | 0.80 | 12 | empty |
| 3 | 93 | 0.42 | 0.78 | 13 | empty |
| 4 | 89 | 0.41 | 0.78 | 17 | empty |
| 5 | 59 | 0.28 | 0.74 | 15 | empty |
Compared structures
- 1H3E · Tyrosyl-tRNA synthetase from Thermus thermophilus complexed with wild-type tRNAtyr(GUA)… · an experimental structure of the same protein · chain A against A, TM-score 0.83
- 1H3E · Tyrosyl-tRNA synthetase from thermus thermophilus complexed with wild- type TRNATYR(GUA)… · an experimental structure of the same protein · chain A against A, TM-score 0.83
- 1H3F · Tyrosyl-tRNA synthetase from Thermus thermophilus complexed with tyrosinol · an experimental structure of the same protein · chain A against B, TM-score 0.79
- 1H3F · Tyrosyl-tRNA synthetase from thermus thermophilus complexed with tyrosinol · an experimental structure of the same protein · chain A against B, TM-score 0.79
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 P83453
- Elsewhere: UniProt P83453 · AlphaFold DB P83453
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