Research workbench
AlphaFold monomer V2.0 prediction for histidinol-phosphate aminotransferase (Q87C30)
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
- Q87C30
- Type
- protein
- Length
- 365 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xB44F19a0cb161828322eEEd13F55d4C3C34938d2
- Molecule
- Histidinol-phosphate aminotransferase
- UniProt
- Q87C30
- Pockets
- 6 · best druggability 0.44
Structure
1 distinct chain · 40% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histidinol-phosphate aminotransferase | protein | 365 | 40% helix, 15% strand | Q87C30 |
Pockets
6 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 54 | 0.44 | 0.84 | 17 | empty |
| 2 | 72 | 0.37 | 0.77 | 25 | empty |
| 3 | 57 | 0.35 | 0.79 | 21 | empty |
| 4 | 53 | 0.34 | 0.78 | 21 | empty |
| 5 | 80 | 0.34 | 0.75 | 20 | 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 Q87C30
- Elsewhere: UniProt Q87C30 · AlphaFold DB Q87C30
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