Research workbench
AlphaFold monomer V2.0 prediction for histidine--tRNA ligase (Q9PPF4)
Analyse AlphaFold monomer V2.0 prediction for histidine--tRNA ligase (Q9PPF4) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9PPF4
- Type
- protein
- Length
- 408 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xba10dCAB85f8E44298b6025C21224eB1B2a215c2
- Molecule
- Histidine--tRNA ligase
- UniProt
- Q9PPF4
- Pockets
- 4 · best druggability 0.75
Structure
1 distinct chain · 41% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histidine--tRNA ligase | protein | 408 | 41% helix, 23% strand | Q9PPF4 |
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 | 564 | 0.75 | 0.82 | 61 | empty |
| 2 | 138 | 0.50 | 0.79 | 24 | empty |
| 3 | 82 | 0.42 | 0.79 | 16 | empty |
| 4 | 50 | 0.27 | 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 Q9PPF4
- Elsewhere: UniProt Q9PPF4 · AlphaFold DB Q9PPF4
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