Research workbench
AlphaFold monomer V2.0 prediction for virulence sensor histidine kinase phoq (Q5PMJ0)
Analyse AlphaFold monomer V2.0 prediction for virulence sensor histidine kinase phoq… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q5PMJ0
- Type
- protein
- Length
- 487 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x35612D34a32C306CA4fc1edA9360D1F717e25950
- Molecule
- Virulence sensor histidine kinase phoq
- UniProt
- Q5PMJ0
- Pockets
- 4 · best druggability 0.68
Structure
1 distinct chain · 52% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Virulence sensor histidine kinase phoq | protein | 487 | 52% helix, 17% strand | Q5PMJ0 |
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 | 390 | 0.68 | 0.81 | 43 | empty |
| 2 | 189 | 0.46 | 0.75 | 20 | empty |
| 3 | 50 | 0.37 | 0.80 | 13 | empty |
| 4 | 52 | 0.28 | 0.75 | 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 Q5PMJ0
- Elsewhere: UniProt Q5PMJ0 · AlphaFold DB Q5PMJ0
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