Research workbench
AlphaFold monomer V2.0 prediction for tyrosine--tRNA ligase (C1CH28)
Analyse AlphaFold monomer V2.0 prediction for tyrosine--tRNA ligase (C1CH28) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- C1CH28
- Type
- protein
- Length
- 418 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xB05a6C07895e32B47A59E248baa07d66d77b0e17
- Molecule
- Tyrosine--tRNA ligase
- UniProt
- C1CH28
- Pockets
- 4 · best druggability 0.76
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 | C1CH28 |
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 | 346 | 0.76 | 0.86 | 47 | empty |
| 2 | 155 | 0.42 | 0.74 | 25 | empty |
| 3 | 104 | 0.39 | 0.75 | 16 | empty |
| 4 | 71 | 0.37 | 0.77 | 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 C1CH28
- Elsewhere: UniProt C1CH28 · AlphaFold DB C1CH28
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