Structure analysis

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

X-ray diffraction
2.9Å resolution
Assemblies composition:
hetero dimer (preferred)
hetero dodecamer
Entry contents: 2 distinct polypeptide molecules

Assemblies

Assembly 1 (preferred)
Download    3D Visualisation
Multimeric state: hetero dimer

Binding statistics and energies are not available for this assembly
Assembly 2
Download    3D Visualisation
Multimeric state: hetero dimer

Binding statistics and energies are not available for this assembly
Assembly 3
Download    3D Visualisation
Multimeric state: hetero dodecamer

Binding statistics and energies are not available for this assembly

Macromolecules

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
Pfam: Isocitrate dehydrogenase kinase/phosphatase (AceK)
InterPro: Isocitrate dehydrogenase kinasephosphatase

Search similar proteins

Chains: C, D
Length: 416 amino acids
Theoretical weight: 45.81 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P08200 (Residues: 1-416; Coverage: 100%)
Gene names: JW1122, b1136, icd, icdA, icdE
Pfam: Isocitrate/isopropylmalate dehydrogenase
InterPro:
CATH: Isopropylmalate Dehydrogenase

Search similar proteins