› 6k5l

X-ray diffraction
2.55Å resolution

The crystal structure of isocitrate dehydrogenase kinase/phosphatase wtih two Mn2+ from E. coli

Released:
DOI: 10.2210/pdb6k5l/pdb
PDB entry 6k5l coloured by chain, front view.
PDB entry 6k5l coloured by chain, side view.
PDB entry 6k5l coloured by chain, top view.
Source organism: Escherichia coli O157
Primary publication:
Characterization of metal binding of bifunctional kinase/phosphatase AceK and implication in activity modulation.
Zhang X, Shen Q, Lei Z, Wang Q, Zheng J, Jia Z
Sci Rep 9 9198 (2019)
PMID: 31235769

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:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145645 (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
Expression system: Escherichia coli
UniProt:
  • Canonical: P11071 (Residues: 1-578; Coverage: 100%)
Gene names: JW3976, aceK, b4016
Sequence domains:

Ligands and Environments

3 bound ligands:
Ligand AMP 2 x AMP
Ligand ADP 2 x ADP
Ligand MN 4 x MN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U1
Spacegroup: P41212
Unit cell:
a: 124.484Å b: 124.484Å c: 266.824Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.193 0.192 0.221
Expression system: Escherichia coli

Quick links

Citations

1 citations in other articles

Expression of the ace operon in Escherichia coli is triggered in response to growth rate-dependent flux-signal of ATP.
El-Mansi et al. (2021)

1 mention without citation

Characterization of metal binding of bifunctional kinase/phosphatase AceK and implication in activity modulation.
Zhang et al. (2019)