Research workbench
AlphaFold monomer V2.0 prediction for biosynthetic arginine decarboxylase (B4F1A4)
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
- B4F1A4
- Type
- protein
- Length
- 635 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xB44F19a0cb161828322eEEd13F55d4C3C34938d2
- Molecule
- Biosynthetic arginine decarboxylase
- UniProt
- B4F1A4
- Pockets
- 4 · best druggability 0.58
Structure
1 distinct chain · 44% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Biosynthetic arginine decarboxylase | protein | 635 | 44% helix, 18% strand | B4F1A4 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 253 | 0.58 | 0.79 | 36 | empty |
| 2 | 200 | 0.53 | 0.78 | 22 | empty |
| 3 | 210 | 0.49 | 0.75 | 26 | empty |
| 4 | 79 | 0.37 | 0.77 | 14 | 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 B4F1A4
- Elsewhere: UniProt B4F1A4 · AlphaFold DB B4F1A4
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