Research workbench
AlphaFold monomer V2.0 prediction for signal transduction histidine- protein KINASE/PHOSPHATASE mprb (A3Q5L8)
Analyse AlphaFold monomer V2.0 prediction for signal transduction histidine- protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A3Q5L8
- Type
- protein
- Length
- 515 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x00bd06314bCF4b41dc8b20EFb04Ad8E3061cf667
- Molecule
- Signal transduction histidine-protein KINASE/PHOSPHATASE mprb
- UniProt
- A3Q5L8
- Pockets
- 3 · best druggability 0.72
Structure
1 distinct chain · 50% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Signal transduction histidine-protein KINASE/PHOSPHATASE mprb | protein | 515 | 50% helix, 15% strand | A3Q5L8 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 294 | 0.72 | 0.85 | 38 | empty |
| 2 | 75 | 0.44 | 0.81 | 18 | empty |
| 3 | 119 | 0.38 | 0.74 | 20 | 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 A3Q5L8
- Elsewhere: UniProt A3Q5L8 · AlphaFold DB A3Q5L8
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