Research workbench
AlphaFold monomer V2.0 prediction for histidinol-phosphate aminotransferase (Q3ARM7)
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
- Q3ARM7
- Type
- protein
- Length
- 363 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xd35252F5c9506AaAf4362F7480283C06BBd38C02
- Molecule
- Histidinol-phosphate aminotransferase
- UniProt
- Q3ARM7
- Pockets
- 5 · best druggability 0.65
Structure
1 distinct chain · 40% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histidinol-phosphate aminotransferase | protein | 363 | 40% helix, 15% strand | Q3ARM7 |
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 251 | 0.65 | 0.82 | 31 | empty |
| 2 | 149 | 0.45 | 0.76 | 27 | empty |
| 3 | 63 | 0.36 | 0.78 | 13 | empty |
| 4 | 58 | 0.31 | 0.76 | 17 | empty |
| 5 | 57 | 0.30 | 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 Q3ARM7
- Elsewhere: UniProt Q3ARM7 · AlphaFold DB Q3ARM7
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