Function and Biology Details
Reaction catalysed:
[a protein]-serine/threonine phosphate + H(2)O = [a protein]-serine/threonine + phosphate
Biochemical function:
Biological process:
- not assigned
Cellular component:
- not assigned
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-131124 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
Molecule details ›
Chains: A, C
Length: 299 amino acids
Theoretical weight: 34.16 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains:
Structure domains: Purple Acid Phosphatase; chain A, domain 2
Length: 299 amino acids
Theoretical weight: 34.16 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
P62136 (Residues: 7-300; Coverage: 89%)
Sequence domains:
Structure domains: Purple Acid Phosphatase; chain A, domain 2
Protein phosphatase 1 regulatory subunit 15A
Molecule details ›
Chains: B, D
Length: 43 amino acids
Theoretical weight: 4.94 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: Phosphatase-1 catalytic subunit binding region
Length: 43 amino acids
Theoretical weight: 4.94 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical: O75807 (Residues: 552-591; Coverage: 6%)
Sequence domains: Phosphatase-1 catalytic subunit binding region
