Research workbench
AlphaFold monomer V2.0 prediction for histidine--tRNA ligase (A2CCR1)
Analyse AlphaFold monomer V2.0 prediction for histidine--tRNA ligase (A2CCR1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A2CCR1
- Type
- protein
- Length
- 436 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x0D671490EE06E75975e90D7F99F73B20BE618744
- Molecule
- Histidine--tRNA ligase
- UniProt
- A2CCR1
- Pockets
- 5 · best druggability 0.74
Structure
1 distinct chain · 44% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histidine--tRNA ligase | protein | 436 | 44% helix, 22% strand | A2CCR1 |
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 524 | 0.74 | 0.83 | 58 | empty |
| 2 | 197 | 0.55 | 0.79 | 31 | empty |
| 3 | 88 | 0.37 | 0.76 | 18 | empty |
| 4 | 73 | 0.32 | 0.74 | 11 | empty |
| 5 | 50 | 0.32 | 0.77 | 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 A2CCR1
- Elsewhere: UniProt A2CCR1 · AlphaFold DB A2CCR1
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