Research workbench
AlphaFold monomer V2.0 prediction for histidine--tRNA ligase (A1V9B1)
Analyse AlphaFold monomer V2.0 prediction for histidine--tRNA ligase (A1V9B1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A1V9B1
- Type
- protein
- Length
- 417 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x44D50E828c22812996CB99C7F2E0C5EC9933b478
- Molecule
- Histidine--tRNA ligase
- UniProt
- A1V9B1
- Pockets
- 3 · best druggability 0.74
Structure
1 distinct chain · 41% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histidine--tRNA ligase | protein | 417 | 41% helix, 22% strand | A1V9B1 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 513 | 0.74 | 0.83 | 59 | empty |
| 2 | 81 | 0.35 | 0.75 | 19 | empty |
| 3 | 89 | 0.34 | 0.75 | 22 | 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 A1V9B1
- Elsewhere: UniProt A1V9B1 · AlphaFold DB A1V9B1
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