PDBe 1s70

X-ray diffraction
2.7Å resolution

Complex between protein ser/thr phosphatase-1 (delta) and the myosin phosphatase targeting subunit 1 (MYPT1)

Source organisms:
Primary publication:
Structural basis of protein phosphatase 1 regulation.
Nature 429 780-4 (2004)
PMID: 15164081

Function and Biology Details

Reactions catalysed:
[Myosin light-chain] phosphate + H(2)O = [myosin light-chain] + phosphate. 
[a protein]-serine/threonine phosphate + H(2)O = [a protein]- serine/threonine + phosphate. 
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Protein phosphatase 1 regulatory subunit 12A Chain: B
Molecule details ›
Chain: B
Length: 299 amino acids
Theoretical weight: 33.36 KDa
Source organism: Gallus gallus
Expression system: Escherichia coli
  • Canonical: Q90623 (Residues: 1-299; Coverage: 30%)
Gene names: MBS, MYPT1, PPP1R12A
Sequence domains: Ankyrin repeats (3 copies)
Structure domains: Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Serine/threonine-protein phosphatase PP1-beta catalytic subunit Chain: A
Molecule details ›
Chain: A
Length: 330 amino acids
Theoretical weight: 37.5 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
  • Canonical: P62207 (Residues: 1-327; Coverage: 100%)
Gene name: PPP1CB
Sequence domains:
Structure domains: Purple Acid Phosphatase; chain A, domain 2

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-C
Spacegroup: P43212
Unit cell:
a: 75.188Å b: 75.188Å c: 241.753Å
α: 90° β: 90° γ: 90°
R R work R free
0.223 0.223 0.293
Expression system: Escherichia coli