Research workbench
AlphaFold monomer V2.0 prediction for histidinol-phosphate aminotransferase (Q1QQD5)
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
- Q1QQD5
- Type
- protein
- Length
- 365 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xbff27Dc0a932A6E0d9Fe883AAbD1BF27bB95A69F
- Molecule
- Histidinol-phosphate aminotransferase
- UniProt
- Q1QQD5
- Pockets
- 4 · best druggability 0.57
Structure
1 distinct chain · 41% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histidinol-phosphate aminotransferase | protein | 365 | 41% helix, 18% strand | Q1QQD5 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 166 | 0.57 | 0.82 | 29 | empty |
| 2 | 102 | 0.35 | 0.73 | 20 | empty |
| 3 | 64 | 0.29 | 0.74 | 18 | empty |
| 4 | 53 | 0.27 | 0.73 | 11 | 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 Q1QQD5
- Elsewhere: UniProt Q1QQD5 · AlphaFold DB Q1QQD5
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