4mp0

X-ray diffraction
2.1Å resolution

Structure of a second nuclear PP1 Holoenzyme, crystal form 2

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-129530 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Serine/threonine-protein phosphatase PP1-alpha catalytic subunit Chains: A, C
Molecule details ›
Chains: A, C
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:
Structure domains: Purple Acid Phosphatase; chain A, domain 2
Serine/threonine-protein phosphatase 1 regulatory subunit 10 Chains: B, D
Molecule details ›
Chains: B, D
Length: 44 amino acids
Theoretical weight: 5.22 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
  • Canonical: O55000 (Residues: 394-433; Coverage: 5%)
Gene names: Cat53, Pnuts, Ppp1r10

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P41212
Unit cell:
a: 92.407Å b: 92.407Å c: 199.342Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.174 0.172 0.202
Expression system: Escherichia coli