› 1it6

X-ray diffraction
2Å resolution

CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN CALYCULIN A AND THE CATALYTIC SUBUNIT OF PROTEIN PHOSPHATASE 1

Released:
DOI: 10.2210/pdb1it6/pdb
PDB entry 1it6 coloured by chain, front view.
PDB entry 1it6 coloured by chain, side view.
PDB entry 1it6 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of the complex between calyculin A and the catalytic subunit of protein phosphatase 1.
Kita A, Matsunaga S, Takai A, Kataiwa H, Wakimoto T, Fusetani N, Isobe M, Miki K
Structure 10 715-24 (2002)
PMID: 12015153

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 Chains: A, B
Molecule details ›
Chains: A, B
Length: 323 amino acids
Theoretical weight: 37.03 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P36873 (Residues: 1-323; Coverage: 100%)
Gene name: PPP1CC
Sequence domains:
Structure domains: Purple Acid Phosphatase; chain A, domain 2

Ligands and Environments

2 bound ligands:
Ligand MN 4 x MN
Ligand CYU 2 x CYU
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44B2
Spacegroup: P21212
Unit cell:
a: 98.09Å b: 136.36Å c: 61.58Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.182 0.182 0.218
Expression system: Escherichia coli

Quick links

Citations

12 review citations

Functional diversity of protein phosphatase-1, a cellular economizer and reset button.
Ceulemans et al. (2004)
11 more

10 mentions without citation

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