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:
Structure domain:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158949 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Serine/threonine-protein phosphatase PP1-gamma catalytic subunit
Molecule details ›
Chains: A, B
Length: 329 amino acids
Theoretical weight: 37.86 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli BL21
UniProt:
Sequence domains:
Structure domains: Purple Acid Phosphatase; chain A, domain 2
Length: 329 amino acids
Theoretical weight: 37.86 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli BL21
UniProt:
- Canonical:
P63088 (Residues: 2-323; Coverage: 100%)
Sequence domains:
Structure domains: Purple Acid Phosphatase; chain A, domain 2
Protein phosphatase inhibitor 2
Molecule details ›
Chains: I, J
Length: 206 amino acids
Theoretical weight: 23.15 KDa
Source organism: Mus musculus
Expression system: Escherichia coli BL21
UniProt:
Sequence domains: Protein phosphatase inhibitor 2 (IPP-2)
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Length: 206 amino acids
Theoretical weight: 23.15 KDa
Source organism: Mus musculus
Expression system: Escherichia coli BL21
UniProt:
- Canonical: Q9DCL8 (Residues: 1-206; Coverage: 100%)
Sequence domains: Protein phosphatase inhibitor 2 (IPP-2)
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
APS BEAMLINE 19-ID
Spacegroup:
P212121
Expression system: Escherichia coli BL21
