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-158555 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
Molecule details ›
Chains: A, C, E, G
Length: 306 amino acids
Theoretical weight: 34.94 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains:
Structure domains: Purple Acid Phosphatase; chain A, domain 2
Length: 306 amino acids
Theoretical weight: 34.94 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
P62136 (Residues: 7-307; Coverage: 91%)
Sequence domains:
Structure domains: Purple Acid Phosphatase; chain A, domain 2
Nuclear inhibitor of protein phosphatase 1
Molecule details ›
Chains: B, D, F, H
Length: 62 amino acids
Theoretical weight: 7.21 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Length: 62 amino acids
Theoretical weight: 7.21 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical: Q12972 (Residues: 158-216; Coverage: 17%)
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces
