› 4moy

X-ray diffraction
2.2Å resolution

Structure of a second nuclear PP1 Holoenzyme, crystal form 1

Released:
DOI: 10.2210/pdb4moy/pdb
PDB entry 4moy coloured by chain, front view.
PDB entry 4moy coloured by chain, side view.
PDB entry 4moy coloured by chain, top view.
Source organisms:
Primary publication:
Understanding the antagonism of retinoblastoma protein dephosphorylation by PNUTS provides insights into the PP1 regulatory code.
Choy MS, Hieke M, Kumar GS, Lewis GR, Gonzalez-DeWhitt KR, Kessler RP, Stein BJ, Hessenberger M, Nairn AC, Peti W, Page R
Proc Natl Acad Sci U S A 111 4097-102 (2014)
PMID: 24591642

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
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-129530 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Serine/threonine-protein phosphatase PP1-alpha catalytic subunit Chain: A
Molecule details ›
Chain: A
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 Chain: B
Molecule details ›
Chain: B
Length: 44 amino acids
Theoretical weight: 5.22 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
  • Canonical: O55000 (Residues: 393-433; Coverage: 5%)
Gene names: Cat53, Pnuts, Ppp1r10

Ligands and Environments

4 bound ligands:
Ligand MN 2 x MN
Ligand CL 1 x CL
Ligand PO4 1 x PO4
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P3221
Unit cell:
a: 130.788Å b: 130.788Å c: 47.725Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.153 0.151 0.185
Expression system: Escherichia coli

Quick links

Citations

11 review citations

Toxin-antitoxin systems in bacterial growth arrest and persistence.
Page et al. (2016)
10 more

9 mentions without citation

Regulation of Three Key Kinases of Brassinosteroid Signaling Pathway.
Mao et al. (2020)
8 more