2iv0

X-ray diffraction
2.5Å resolution

Thermal stability of isocitrate dehydrogenase from Archaeoglobus fulgidus studied by crystal structure analysis and engineering of chimers

Released:
Model geometry
Fit model/data

Function and Biology Details

Reaction catalysed:
(1a) isocitrate + NADP(+) = 2-oxalosuccinate + NADPH
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-128149 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Isocitrate dehydrogenase [NADP] Chains: A, B
Molecule details ›
Chains: A, B
Length: 412 amino acids
Theoretical weight: 45.9 KDa
Source organism: Archaeoglobus fulgidus
Expression system: Escherichia coli
UniProt:
  • Canonical: O29610 (Residues: 1-412; Coverage: 100%)
Gene names: AF_0647, icd
Sequence domains: Isocitrate/isopropylmalate dehydrogenase
Structure domains: Isopropylmalate Dehydrogenase

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P21
Unit cell:
a: 81.611Å b: 65.405Å c: 87.181Å
α: 90° β: 95.28° γ: 90°
R-values:
R R work R free
0.199 0.196 0.254
Expression system: Escherichia coli