6zef

X-ray diffraction
1.94Å resolution

Structure of PP1(7-300) bound to Phactr1 (516-580) at pH 5.25

Released:

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)
PDBe Complex ID:
PDB-CPX-158561 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Serine/threonine-protein phosphatase PP1-alpha catalytic subunit Chains: A, B
Molecule details ›
Chains: A, B
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%)
Gene names: PPP1A, PPP1CA
Sequence domains:
Phosphatase and actin regulator 1 Chains: C, D
Molecule details ›
Chains: C, D
Length: 70 amino acids
Theoretical weight: 8.26 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9C0D0 (Residues: 516-580; Coverage: 11%)
Gene names: KIAA1733, PHACTR1, RPEL1

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: P1
Unit cell:
a: 47.51Å b: 57.55Å c: 89.614Å
α: 78.076° β: 74.673° γ: 81.66°
R-values:
R R work R free
0.183 0.182 0.212
Expression system: Escherichia coli