3lcb

X-ray diffraction
2.9Å resolution

The crystal structure of isocitrate dehydrogenase kinase/phosphatase in complex with its substrate, isocitrate dehydrogenase, from Escherichia coli.

Released:

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
hetero dodecamer
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
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:
  • Best match: Q8X607 (Residues: 1-578)
Gene names: ECs4934, Z5602, aceK
Isocitrate dehydrogenase [NADP] Chains: C, D
Molecule details ›
Chains: C, D
Length: 416 amino acids
Theoretical weight: 45.81 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Best match: P08200 (Residues: 1-416)
Gene names: JW1122, b1136, icd, icdA, icdE

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE A1
Spacegroup: P63
Unit cell:
a: 196.801Å b: 196.801Å c: 156.458Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.192 0.19 0.222
Expression system: Escherichia coli