Research workbench
AlphaFold monomer V2.0 prediction for biosynthetic arginine decarboxylase (B1KRD4)
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
- B1KRD4
- Type
- protein
- Length
- 637 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x4E86D2439266DCa1580a1734488545A520deFE4E
- Molecule
- Biosynthetic arginine decarboxylase
- UniProt
- B1KRD4
- Pockets
- 5 · best druggability 0.65
Structure
1 distinct chain · 45% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Biosynthetic arginine decarboxylase | protein | 637 | 45% helix, 18% strand | B1KRD4 |
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 | 295 | 0.65 | 0.81 | 41 | empty |
| 2 | 50 | 0.46 | 0.86 | 17 | empty |
| 3 | 113 | 0.40 | 0.76 | 30 | empty |
| 4 | 98 | 0.35 | 0.74 | 17 | empty |
| 5 | 86 | 0.34 | 0.74 | 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 B1KRD4
- Elsewhere: UniProt B1KRD4 · AlphaFold DB B1KRD4
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