Function and Biology Details
Reactions catalysed:
[a protein]-serine/threonine phosphate + H(2)O = [a protein]-serine/threonine + phosphate
[Myosin light-chain] phosphate + H(2)O = [myosin light-chain] + phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158592 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Serine/threonine-protein phosphatase PP1-beta catalytic subunit
Molecule details ›
Chain: A
Length: 330 amino acids
Theoretical weight: 37.5 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains:
Structure domains: Purple Acid Phosphatase; chain A, domain 2
Length: 330 amino acids
Theoretical weight: 37.5 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
P62207 (Residues: 1-327; Coverage: 100%)
Sequence domains:
Structure domains: Purple Acid Phosphatase; chain A, domain 2
Protein phosphatase 1 regulatory subunit 12A
Molecule details ›
Chain: B
Length: 299 amino acids
Theoretical weight: 33.36 KDa
Source organism: Gallus gallus
Expression system: Escherichia coli
UniProt:
Sequence domains: Ankyrin repeats (3 copies)
Structure domains: Ankyrin repeat-containing domain
Length: 299 amino acids
Theoretical weight: 33.36 KDa
Source organism: Gallus gallus
Expression system: Escherichia coli
UniProt:
- Canonical: Q90623 (Residues: 1-299; Coverage: 30%)
Sequence domains: Ankyrin repeats (3 copies)
Structure domains: Ankyrin repeat-containing domain
