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-151655 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform
Molecule details ›
Chain: A
Length: 589 amino acids
Theoretical weight: 65.38 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: HEAT repeat
Structure domains: Leucine-rich Repeat Variant
Length: 589 amino acids
Theoretical weight: 65.38 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
P30153 (Residues: 1-589; Coverage: 100%)
Sequence domains: HEAT repeat
Structure domains: Leucine-rich Repeat Variant
Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform
Molecule details ›
Chain: C
Length: 309 amino acids
Theoretical weight: 35.64 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
Sequence domains: Calcineurin-like phosphoesterase
Structure domains: Purple Acid Phosphatase; chain A, domain 2
Length: 309 amino acids
Theoretical weight: 35.64 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
- Canonical: P67775 (Residues: 1-309; Coverage: 100%)
Sequence domains: Calcineurin-like phosphoesterase
Structure domains: Purple Acid Phosphatase; chain A, domain 2
