Research workbench
AlphaFold monomer V2.0 prediction for histidine--tRNA ligase (A5D3E2)
Analyse AlphaFold monomer V2.0 prediction for histidine--tRNA ligase (A5D3E2) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A5D3E2
- Type
- protein
- Length
- 425 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5BeA89782341f98147F2D811B063F91F0aE7D7bF
- Molecule
- Histidine--tRNA ligase
- UniProt
- A5D3E2
- Pockets
- 4 · 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 | 425 | 41% helix, 22% strand | A5D3E2 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 643 | 0.74 | 0.81 | 62 | empty |
| 2 | 92 | 0.55 | 0.85 | 19 | empty |
| 3 | 79 | 0.38 | 0.77 | 17 | empty |
| 4 | 58 | 0.28 | 0.74 | 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 A5D3E2
- Elsewhere: UniProt A5D3E2 · AlphaFold DB A5D3E2
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