› 2pnq

X-ray diffraction
1.81Å resolution

Crystal structure of pyruvate dehydrogenase phosphatase 1 (PDP1)

Released:
DOI: 10.2210/pdb2pnq/pdb
PDB entry 2pnq coloured by chain, front view.
PDB entry 2pnq coloured by chain, side view.
PDB entry 2pnq coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Crystal structure of pyruvate dehydrogenase phosphatase 1 and its functional implications.
Vassylyev DG, Symersky J
J Mol Biol 370 417-26 (2007)
PMID: 17532339

Function and Biology Details

Reaction catalysed: 
[Pyruvate dehydrogenase (acetyl-transferring)] phosphate + H(2)O = [pyruvate dehydrogenase (acetyl-transferring)] + phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-131544 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
[Pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 1, mitochondrial Chains: A, B
Molecule details ›
Chains: A, B
Length: 467 amino acids
Theoretical weight: 52.68 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O88483 (Residues: 72-538; Coverage: 87%)
Gene names: Pdp1, Ppm2c
Sequence domains: Protein phosphatase 2C
Structure domains: PPM-type phosphatase domain

Ligands and Environments

1 bound ligand:
Ligand MG 4 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P21
Unit cell:
a: 65.318Å b: 72.22Å c: 96.094Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.218 0.215 0.256
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

6 review citations

Role of mitochondrial Ca2+ in the regulation of cellular energetics.
Glancy et al. (2012)
5 more

7 mentions without citation

Tyr-94 phosphorylation inhibits pyruvate dehydrogenase phosphatase 1 and promotes tumor growth.
Shan et al. (2014)
6 more