Function and Biology Details
Reaction catalysed:
[a protein]-serine/threonine phosphate + H(2)O = [a protein]-serine/threonine + phosphate
Biochemical function:
- not assigned
Biological process:
- not assigned
Cellular component:
- not assigned
Structure analysis Details
Assembly composition:
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-292291 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Maltodextrin-binding protein
Molecule details ›
Chain: A
Length: 376 amino acids
Theoretical weight: 40.81 KDa
Source organism: Escherichia coli #1/H766
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'
UniProt:
Sequence domains: Bacterial extracellular solute-binding protein
Length: 376 amino acids
Theoretical weight: 40.81 KDa
Source organism: Escherichia coli #1/H766
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'
UniProt:
- Canonical:
A0A4P1LXE0 (Residues: 3-371; Coverage: 79%)
Sequence domains: Bacterial extracellular solute-binding protein
Calmodulin
Molecule details ›
Chain: N
Length: 153 amino acids
Theoretical weight: 17.12 KDa
Source organism: Drosophila melanogaster
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'
UniProt:
Sequence domains: EF-hand domain pair
Length: 153 amino acids
Theoretical weight: 17.12 KDa
Source organism: Drosophila melanogaster
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'
UniProt:
- Canonical: P62152 (Residues: 1-149; Coverage: 100%)
Sequence domains: EF-hand domain pair
Serine/threonine-protein phosphatase rdgC
