› 3lc6

X-ray diffraction
3.1Å resolution

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

Released:
DOI: 10.2210/pdb3lc6/pdb
PDB entry 3lc6 coloured by chain, front view.
PDB entry 3lc6 coloured by chain, side view.
PDB entry 3lc6 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

Assemblies composition:
homo dimer (preferred)
monomeric
Assembly name:
PDBe Complex ID:
PDB-CPX-186844 (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: 67.82 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:

Ligands and Environments

3 bound ligands:
Ligand ADP 1 x ADP
Ligand MG 1 x MG
Ligand AMP 1 x AMP
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

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Citations

8 review citations

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

1 mention without citation

Aromatic interactions at the ligand-protein interface: Implications for the development of docking scoring functions.
Brylinski M. (2018)