› 3eps

X-ray diffraction
2.8Å resolution

The crystal structure of isocitrate dehydrogenase kinase/phosphatase from E. coli

Released:
DOI: 10.2210/pdb3eps/pdb
PDB entry 3eps coloured by chain, front view.
PDB entry 3eps coloured by chain, side view.
PDB entry 3eps coloured by chain, top view.
Source organism: Escherichia coli O157:H7
Primary publication:
Structure of the bifunctional isocitrate dehydrogenase kinase/phosphatase.
Zheng J, Jia Z
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:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-186843 (preferred)
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: 67.78 KDa
Source organism: Escherichia coli O157:H7
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8X607 (Residues: 2-578; Coverage: 100%)
Gene names: ECs4934, Z5602, aceK
Sequence domains:

Ligands and Environments

3 bound ligands:
Ligand AMP 2 x AMP
Ligand ATP 2 x ATP
Ligand MG 2 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE F1
Spacegroup: P41212
Unit cell:
a: 124.595Å b: 124.595Å c: 267.635Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.233 0.233 0.268
Expression system: Escherichia coli

Quick links

Citations

7 review citations

Nitrogen assimilation in Escherichia coli: putting molecular data into a systems perspective.
van Heeswijk et al. (2013)
6 more

4 mentions without citation

Structural and mechanistic insights into the bifunctional enzyme isocitrate dehydrogenase kinase/phosphatase AceK.
Zheng et al. (2012)
3 more