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:
Sequence domains:
- Serine/threonine-specific protein phosphatase/bis(5-nucleosyl)-tetraphosphatase
- SH3 domain
- Ankyrin repeat
- Ankyrin repeat-containing domain superfamily
- Metallo-dependent phosphatase-like
- SH3-like domain superfamily
- Apoptosis-stimulating of p53 protein 1/2
- Calcineurin-like phosphoesterase domain, ApaH type
1 more domain
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158556 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
Molecule details ›
Chains: A, B
Length: 329 amino acids
Theoretical weight: 37.35 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains:
Structure domains: Purple Acid Phosphatase; chain A, domain 2
Length: 329 amino acids
Theoretical weight: 37.35 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
P62136 (Residues: 7-330; Coverage: 98%)
Sequence domains:
Structure domains: Purple Acid Phosphatase; chain A, domain 2
Apoptosis-stimulating of p53 protein 2
Molecule details ›
Chains: C, D
Length: 214 amino acids
Theoretical weight: 24.16 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains:
Structure domains:
Length: 214 amino acids
Theoretical weight: 24.16 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical: Q13625 (Residues: 920-1128; Coverage: 19%)
Sequence domains:
Structure domains:
