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 analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-147677 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Serine/threonine-protein phosphatase 2B catalytic subunit beta isoform
Molecule details ›
Chain: A
Length: 544 amino acids
Theoretical weight: 61.26 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: 544 amino acids
Theoretical weight: 61.26 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
P16298 (Residues: 1-524; 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: 170 amino acids
Theoretical weight: 19.32 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: EF-hand domain pair
Structure domains: EF-hand
Length: 170 amino acids
Theoretical weight: 19.32 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical: P63098 (Residues: 1-170; Coverage: 100%)
Sequence domains: EF-hand domain pair
Structure domains: EF-hand
