› 1u32

X-ray diffraction
2Å resolution

Crystal structure of a Protein Phosphatase-1: Calcineurin Hybrid Bound to Okadaic Acid

Released:
DOI: 10.2210/pdb1u32/pdb
PDB entry 1u32 coloured by chain, front view.
PDB entry 1u32 coloured by chain, side view.
PDB entry 1u32 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure and mutagenesis of a protein phosphatase-1:calcineurin hybrid elucidate the role of the beta12-beta13 loop in inhibitor binding.
Maynes JT, Perreault KR, Cherney MM, Luu HA, James MN, Holmes CF
J Biol Chem 279 43198-206 (2004)
PMID: 15280359

Function and Biology Details

Reaction catalysed: 
[a protein]-serine/threonine phosphate + H(2)O = [a protein]-serine/threonine + phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153234 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine/threonine-protein phosphatase PP1-gamma catalytic subunit Chain: A
Molecule details ›
Chain: A
Length: 293 amino acids
Theoretical weight: 33.77 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P36873 (Residues: 6-298; Coverage: 91%)
Gene name: PPP1CC
Sequence domains:
Structure domains: Purple Acid Phosphatase; chain A, domain 2

Ligands and Environments

3 bound ligands:
Ligand MN 2 x MN
Ligand OKA 1 x OKA
Ligand BME 3 x BME
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: P42212
Unit cell:
a: 98.759Å b: 98.759Å c: 62.18Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.22 0.218 0.254
Expression system: Escherichia coli

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Citations

3 review citations

Structural basis for protein phosphatase 1 regulation and specificity.
Peti et al. (2013)
2 more