5zt0

X-ray diffraction
3.32Å resolution

Crystal Structure of Protein Phosphate 1 Complexed with PP1 binding domain of GL

Released:
Source organisms:

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

Assemblies composition:
hetero dimer (preferred)
monomeric
PDBe Complex ID:
PDB-CPX-158566 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Serine/threonine-protein phosphatase PP1-alpha catalytic subunit Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 294 amino acids
Theoretical weight: 33.72 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P62137 (Residues: 7-300; Coverage: 89%)
Gene names: Ppp1a, Ppp1ca
Sequence domains:
Structure domains: Purple Acid Phosphatase; chain A, domain 2
Protein phosphatase 1 regulatory subunit 3B Chains: G, H, I, J
Molecule details ›
Chains: G, H, I, J
Length: 75 amino acids
Theoretical weight: 8.23 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q86XI6 (Residues: 31-105; Coverage: 26%)
Gene names: PPP1R3B, PPP1R4

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL19U1
Spacegroup: P32
Unit cell:
a: 106.53Å b: 106.53Å c: 187.51Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.202 0.2 0.233
Expression system: Escherichia coli