› 1ika

X-ray diffraction
2.7Å resolution

STRUCTURE OF ISOCITRATE DEHYDROGENASE WITH ALPHA-KETOGLUTARATE AT 2.7 ANGSTROMS RESOLUTION: CONFORMATIONAL CHANGES INDUCED BY DECARBOXYLATION OF ISOCITRATE

Released:
DOI: 10.2210/pdb1ika/pdb
PDB entry 1ika coloured by chain, front view.
PDB entry 1ika coloured by chain, side view.
PDB entry 1ika coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structure of isocitrate dehydrogenase with alpha-ketoglutarate at 2.7-A resolution: conformational changes induced by decarboxylation of isocitrate.
Stoddard BL, Koshland DE
Biochemistry 32 9317-22 (1993)
PMID: 8369301

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140025 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Isocitrate dehydrogenase [NADP] Chain: A
Molecule details ›
Chain: A
Length: 416 amino acids
Theoretical weight: 45.81 KDa
Source organism: Escherichia coli
Expression system: Not provided
UniProt:
  • Canonical: P08200 (Residues: 1-416; Coverage: 100%)
Gene names: JW1122, b1136, icd, icdA, icdE
Sequence domains: Isocitrate/isopropylmalate dehydrogenase
Structure domains: Isopropylmalate Dehydrogenase

Ligands and Environments

2 bound ligands:
Ligand CA 1 x CA
Ligand AKG 1 x AKG
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P43212
Unit cell:
a: 105.1Å b: 105.1Å c: 150.3Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.185 0.185 not available
Expression system: Not provided

Quick links

Citations

4 review citations

New Perspectives in Treating Acute Myeloid Leukemia: Driving towards a Patient-Tailored Strategy.
Andreozzi et al. (2022)
3 more

1 mention without citation

Induced fit and the catalytic mechanism of isocitrate dehydrogenase.
Gonçalves et al. (2012)