Research workbench
AlphaFold monomer V2.0 prediction for biosynthetic arginine decarboxylase (Q8PFQ5)
Analyse AlphaFold monomer V2.0 prediction for biosynthetic arginine decarboxylase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q8PFQ5
- Type
- protein
- Length
- 628 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x4d07E6a23DeB6B95bd9b90EcB67368b7e8D3B77e
- Molecule
- Biosynthetic arginine decarboxylase
- UniProt
- Q8PFQ5
- Pockets
- 3 · best druggability 0.54
Structure
1 distinct chain · 43% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Biosynthetic arginine decarboxylase | protein | 628 | 43% helix, 17% strand | Q8PFQ5 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 83 | 0.54 | 0.85 | 16 | empty |
| 2 | 222 | 0.52 | 0.77 | 35 | empty |
| 3 | 100 | 0.48 | 0.81 | 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 Q8PFQ5
- Elsewhere: UniProt Q8PFQ5 · AlphaFold DB Q8PFQ5
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