› 5l58

X-ray diffraction
3.04Å 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 Chain: A
Molecule details ›
Chain: A
Length: 414 amino acids
Theoretical weight: 46.41 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 1 x NDP
1 bound ligand:
Ligand 6MX 1 x 6MX
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04-1
Spacegroup: P43212
Unit cell:
a: 72.166Å b: 72.166Å c: 179.829Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.232 0.23 0.264
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Inhibition of Glycolysis and Glutaminolysis: An Emerging Drug Discovery Approach to Combat Cancer.
Akins et al. (2018)
3 more

2 mentions without citation

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