Research workbench
AlphaFold monomer V2.0 prediction for biosynthetic arginine decarboxylase (A9N4N1)
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
- A9N4N1
- Type
- protein
- Length
- 632 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x362a6d063b1B7E1B6EfD3A9A7CA3612e3FE037AA
- Molecule
- Biosynthetic arginine decarboxylase
- UniProt
- A9N4N1
- Pockets
- 4 · best druggability 0.56
Structure
1 distinct chain · 44% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Biosynthetic arginine decarboxylase | protein | 632 | 44% helix, 17% strand | A9N4N1 |
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 | 213 | 0.56 | 0.79 | 33 | empty |
| 2 | 88 | 0.45 | 0.80 | 20 | empty |
| 3 | 131 | 0.41 | 0.75 | 23 | empty |
| 4 | 61 | 0.28 | 0.74 | 13 | 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 A9N4N1
- Elsewhere: UniProt A9N4N1 · AlphaFold DB A9N4N1
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