3lc6

X-ray diffraction
3.1Å resolution

The alternative conformation structure of isocitrate dehydrogenase kinase/phosphatase from E. Coli

Released:
Source organism: Escherichia coli O157:H7
Primary publication:
Structure of the bifunctional isocitrate dehydrogenase kinase/phosphatase.
Nature 465 961-5 (2010)
PMID: 20505668

Function and Biology Details

Reaction catalysed:
ATP + [isocitrate dehydrogenase (NADP(+))] = ADP + [isocitrate dehydrogenase (NADP(+))] phosphate
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
monomeric
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Isocitrate dehydrogenase kinase/phosphatase Chains: A, B
Molecule details ›
Chains: A, B
Length: 578 amino acids
Theoretical weight: 67.82 KDa
Source organism: Escherichia coli O157:H7
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8X607 (Residues: 1-578; Coverage: 100%)
Gene names: ECs4934, Z5602, aceK
Sequence domains: Isocitrate dehydrogenase kinase/phosphatase (AceK)

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE F1
Spacegroup: P212121
Unit cell:
a: 64.145Å b: 133.757Å c: 187.339Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.289 0.287 0.332
Expression system: Escherichia coli