› 5tqh

X-ray diffraction
2.2Å resolution

Function and Biology Details

Reaction catalysed: 
(1a) isocitrate + NADP(+) = 2-oxalosuccinate + NADPH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-131150 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Isocitrate dehydrogenase [NADP] cytoplasmic Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 417 amino acids
Theoretical weight: 46.91 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O75874 (Residues: 1-414; Coverage: 100%)
Gene names: IDH1, PICD
Sequence domains: Isocitrate/isopropylmalate dehydrogenase
Structure domains: Isopropylmalate Dehydrogenase

Ligands and Environments


Cofactor: Ligand NDP 4 x NDP
2 bound ligands:
Ligand FLC 4 x FLC
Ligand 7J2 4 x 7J2
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P212121
Unit cell:
a: 81.731Å b: 155.745Å c: 163.048Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.188 0.225
Expression system: Escherichia coli

Quick links

Citations

9 review citations

Mutant Isocitrate Dehydrogenase Inhibitors as Targeted Cancer Therapeutics.
Golub et al. (2019)
8 more

9 mentions without citation

Recent advances of IDH1 mutant inhibitor in cancer therapy.
Tian et al. (2022)
8 more