Research workbench
AlphaFold monomer V2.0 prediction for histidinol-phosphate aminotransferase (Q8FNZ1)
Analyse AlphaFold monomer V2.0 prediction for histidinol-phosphate aminotransferase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q8FNZ1
- Type
- protein
- Length
- 372 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x4A5C978525ad251797e983213Fa9aD0A9E376C59
- Molecule
- Histidinol-phosphate aminotransferase
- UniProt
- Q8FNZ1
- Pockets
- 3 · best druggability 0.61
Structure
1 distinct chain · 43% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histidinol-phosphate aminotransferase | protein | 372 | 43% helix, 15% strand | Q8FNZ1 |
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 | 262 | 0.61 | 0.80 | 40 | empty |
| 2 | 77 | 0.31 | 0.74 | 17 | empty |
| 3 | 57 | 0.27 | 0.73 | 17 | 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 Q8FNZ1
- Elsewhere: UniProt Q8FNZ1 · AlphaFold DB Q8FNZ1
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