Research workbench
AlphaFold monomer V2.0 prediction for histidine--tRNA ligase (A8GMY5)
Analyse AlphaFold monomer V2.0 prediction for histidine--tRNA ligase (A8GMY5) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A8GMY5
- Type
- protein
- Length
- 415 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x0D671490EE06E75975e90D7F99F73B20BE618744
- Molecule
- Histidine--tRNA ligase
- UniProt
- A8GMY5
- Pockets
- 3 · best druggability 0.75
Structure
1 distinct chain · 42% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histidine--tRNA ligase | protein | 415 | 42% helix, 21% strand | A8GMY5 |
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 | 588 | 0.75 | 0.82 | 59 | empty |
| 2 | 89 | 0.45 | 0.80 | 25 | empty |
| 3 | 107 | 0.39 | 0.76 | 19 | 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 A8GMY5
- Elsewhere: UniProt A8GMY5 · AlphaFold DB A8GMY5
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