Research workbench
AlphaFold monomer V2.0 prediction for arginine decarboxylase (P49726)
Analyse AlphaFold monomer V2.0 prediction for arginine decarboxylase (P49726) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P49726
- Type
- protein
- Length
- 502 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xa73BAb1DabE4333A884D03393eAa10c3B4215494
- Molecule
- Arginine decarboxylase
- UniProt
- P49726
- Pockets
- 5 · best druggability 0.54
Structure
1 distinct chain · 45% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Arginine decarboxylase | protein | 502 | 45% helix, 17% strand | P49726 |
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 | 213 | 0.54 | 0.78 | 35 | empty |
| 2 | 57 | 0.44 | 0.84 | 21 | empty |
| 3 | 69 | 0.40 | 0.79 | 14 | empty |
| 4 | 67 | 0.32 | 0.75 | 16 | empty |
| 5 | 53 | 0.31 | 0.76 | 15 | 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 P49726
- Elsewhere: UniProt P49726 · AlphaFold DB P49726
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