Research workbench
AlphaFold monomer V2.0 prediction for histidine--tRNA ligase (A8EZE6)
Analyse AlphaFold monomer V2.0 prediction for histidine--tRNA ligase (A8EZE6) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A8EZE6
- Type
- protein
- Length
- 415 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xF8cD1d8d93E9783063700De244A6e3cf6A195579
- Molecule
- Histidine--tRNA ligase
- UniProt
- A8EZE6
- Pockets
- 3 · best druggability 0.73
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 | A8EZE6 |
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 | 624 | 0.73 | 0.81 | 60 | empty |
| 2 | 123 | 0.42 | 0.76 | 22 | empty |
| 3 | 66 | 0.36 | 0.78 | 23 | 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 A8EZE6
- Elsewhere: UniProt A8EZE6 · AlphaFold DB A8EZE6
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