Function and Biology Details
Reactions catalysed:
Peptidylproline (omega=180) = peptidylproline (omega=0)
[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-159230 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Serine/threonine-protein phosphatase 2A activator
Molecule details ›
Chains: A, B
Length: 304 amino acids
Theoretical weight: 34.86 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: Phosphotyrosyl phosphate activator (PTPA) protein
Structure domains: Four Helix Bundle (Hemerythrin (Met), subunit A)
Length: 304 amino acids
Theoretical weight: 34.86 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
Q15257 (Residues: 22-358; Coverage: 84%)
Sequence domains: Phosphotyrosyl phosphate activator (PTPA) protein
Structure domains: Four Helix Bundle (Hemerythrin (Met), subunit A)
Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform
Molecule details ›
Chains: C, D
Length: 6 amino acids
Theoretical weight: 755 Da
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
Length: 6 amino acids
Theoretical weight: 755 Da
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
- Canonical: P67775 (Residues: 304-309; Coverage: 2%)
