Research workbench
AlphaFold monomer V2.0 prediction for fosmidomycin resistance protein (P52067)
Analyse AlphaFold monomer V2.0 prediction for fosmidomycin resistance protein (P52067) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P52067
- Type
- protein
- Length
- 406 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xFE04EC045E1BA245Bec1eE3dfF31a8B2Daf70d91
- Molecule
- Fosmidomycin resistance protein
- UniProt
- P52067
- Pockets
- 4 · best druggability 0.80
Structure
1 distinct chain · 81% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fosmidomycin resistance protein | protein | 406 | 81% helix, 0% strand | P52067 |
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 | 860 | 0.80 | 0.82 | 75 | empty |
| 2 | 360 | 0.55 | 0.74 | 28 | empty |
| 3 | 104 | 0.43 | 0.78 | 18 | empty |
| 4 | 52 | 0.29 | 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 P52067
- Elsewhere: UniProt P52067 · AlphaFold DB P52067
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