Function and Biology Details
Reaction catalysed:
[a protein]-serine/threonine phosphate + H(2)O = [a protein]-serine/threonine + phosphate
Biochemical function:
Biological process:
Cellular component:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153238 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Serine/threonine-protein phosphatase PP1-gamma catalytic subunit
Molecule details ›
Chain: A
Length: 305 amino acids
Theoretical weight: 35.04 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains:
Structure domains: Purple Acid Phosphatase; chain A, domain 2
Length: 305 amino acids
Theoretical weight: 35.04 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
P36873 (Residues: 7-308; Coverage: 94%)
Sequence domains:
Structure domains: Purple Acid Phosphatase; chain A, domain 2
Cell division cycle-associated protein 2
Molecule details ›
Chain: B
Length: 46 amino acids
Theoretical weight: 5.09 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: Protein phosphatase 1 binding
Length: 46 amino acids
Theoretical weight: 5.09 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical: Q69YH5 (Residues: 383-423; Coverage: 4%)
Sequence domains: Protein phosphatase 1 binding
