› 1jm6

X-ray diffraction
2.5Å resolution

Pyruvate dehydrogenase kinase, isozyme 2, containing ADP

Released:
DOI: 10.2210/pdb1jm6/pdb
PDB entry 1jm6 coloured by chain, front view.
PDB entry 1jm6 coloured by chain, side view.
PDB entry 1jm6 coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Structure of pyruvate dehydrogenase kinase. Novel folding pattern for a serine protein kinase.
Steussy CN, Popov KM, Bowker-Kinley MM, Sloan RB, Harris RA, Hamilton JA
J Biol Chem 276 37443-50 (2001)
PMID: 11483605

Function and Biology Details

Reaction catalysed: 
ATP + [pyruvate dehydrogenase (acetyl-transferring)] = ADP + [pyruvate dehydrogenase (acetyl-transferring)] phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-179145 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
[Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 2, mitochondrial Chains: A, B
Molecule details ›
Chains: A, B
Length: 407 amino acids
Theoretical weight: 46.16 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q64536 (Residues: 1-407; Coverage: 100%)
Gene name: Pdk2
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand MG 2 x MG
Ligand ADP 2 x ADP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300, NSLS BEAMLINE X12C
Spacegroup: P21
Unit cell:
a: 71.421Å b: 109.874Å c: 71.414Å
α: 90° β: 104.52° γ: 90°
R-values:
R R work R free
0.19 0.202 0.262
Expression system: Escherichia coli

Quick links

Citations

10 review citations

Regulation of pyruvate metabolism and human disease.
Gray et al. (2014)
9 more

8 mentions without citation

Peptides and peptidomimetics as regulators of protein-protein interactions.
Cunningham et al. (2017)
7 more