Research workbench
AlphaFold monomer V2.0 prediction for polyamine aminopropyltransferase (A9R1H4)
Analyse AlphaFold monomer V2.0 prediction for polyamine aminopropyltransferase (A9R1H4) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A9R1H4
- Type
- protein
- Length
- 296 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xBF0D2e107Ce1EcD2C4369B042274201DB719AaAF
- Molecule
- Polyamine aminopropyltransferase
- UniProt
- A9R1H4
- Pockets
- 1 · best druggability 0.78
Structure
1 distinct chain · 35% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Polyamine aminopropyltransferase | protein | 296 | 35% helix, 28% strand | A9R1H4 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 454 | 0.78 | 0.86 | 52 | 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 A9R1H4
- Elsewhere: UniProt A9R1H4 · AlphaFold DB A9R1H4
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