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:
- EF-hand domain
- Serine/threonine-specific protein phosphatase/bis(5-nucleosyl)-tetraphosphatase
- EF-Hand 1, calcium-binding site
- Metallo-dependent phosphatase-like
- EF-hand domain pair
- Calcineurin B protein
- Calcineurin-like phosphoesterase domain, ApaH type
- PP2B, metallophosphatase domain
1 more domain
Structure domains:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158960 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Protein phosphatase 3 catalytic subunit alpha
Molecule details ›
Chain: A
Length: 521 amino acids
Theoretical weight: 58.76 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: Calcineurin-like phosphoesterase
Structure domains: Purple Acid Phosphatase; chain A, domain 2
Length: 521 amino acids
Theoretical weight: 58.76 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
Q08209 (Residues: 1-521; Coverage: 100%)
Sequence domains: Calcineurin-like phosphoesterase
Structure domains: Purple Acid Phosphatase; chain A, domain 2
Calcineurin subunit B type 1
Molecule details ›
Chain: B
Length: 169 amino acids
Theoretical weight: 19.19 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: EF-hand domain pair
Structure domains: EF-hand
Length: 169 amino acids
Theoretical weight: 19.19 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical: P63098 (Residues: 2-170; Coverage: 99%)
Sequence domains: EF-hand domain pair
Structure domains: EF-hand
