Structure analysis

REGULATORY AND CATALYTIC MECHANISMS IN ESCHERICHIA COLI ISOCITRATE DEHYDROGENASE: MULTIPLE ROLES FOR N115

X-ray diffraction
2.5Å resolution
Source organism: Escherichia coli
Assembly composition:
homo dimer (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
Download    3D Visualisation
Multimeric state: homo dimer
Accessible surface area: 30515.13 Å2
Buried surface area: 7699.27 Å2
Dissociation area: 3,392.84 Å2
Dissociation energy (ΔGdiss): 52.55 kcal/mol
Dissociation entropy (TΔSdiss): 14.9 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-140025

Macromolecules

Chain: A
Length: 416 amino acids
Theoretical weight: 45.84 KDa
Source organism: Escherichia coli
Expression system: Not provided
UniProt:
  • Canonical: P08200 (Residues: 1-416; Coverage: 100%)
Gene names: JW1122, b1136, icd, icdA, icdE
Pfam: Isocitrate/isopropylmalate dehydrogenase
InterPro:
CATH: Isopropylmalate Dehydrogenase
SCOP: Dimeric isocitrate & isopropylmalate dehydrogenases

Search similar proteins