Function and Biology Details
Reaction catalysed:
[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-158559 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
Molecule details ›
Chains: A, C
Length: 299 amino acids
Theoretical weight: 34.16 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains:
Structure domains: Purple Acid Phosphatase; chain A, domain 2
Length: 299 amino acids
Theoretical weight: 34.16 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
P62136 (Residues: 7-300; Coverage: 89%)
Sequence domains:
Structure domains: Purple Acid Phosphatase; chain A, domain 2
Cell division cycle-associated protein 2
Molecule details ›
Chains: B, D
Length: 64 amino acids
Theoretical weight: 7.02 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: Protein phosphatase 1 binding
Length: 64 amino acids
Theoretical weight: 7.02 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical: Q69YH5 (Residues: 383-441; Coverage: 6%)
Sequence domains: Protein phosphatase 1 binding
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
NSLS BEAMLINE X25
Spacegroup:
P21212
Expression system: Escherichia coli
