› 1cw4

X-ray diffraction
2.1Å resolution

CRYSTAL STRUCTURE OF K230M ISOCITRATE DEHYDROGENASE IN COMPLEX WITH ALPHA-KETOGLUTARATE

Released:
DOI: 10.2210/pdb1cw4/pdb
PDB entry 1cw4 coloured by chain, front view.
PDB entry 1cw4 coloured by chain, side view.
PDB entry 1cw4 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Active site water molecules revealed in the 2.1 A resolution structure of a site-directed mutant of isocitrate dehydrogenase.
Cherbavaz DB, Lee ME, Stroud RM, Koshland DE
J Mol Biol 295 377-85 (2000)
PMID: 10623532

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: Escherichia coli
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

3 bound ligands:
Ligand MN 1 x MN
Ligand SO4 1 x SO4
Ligand AKG 1 x AKG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: P43212
Unit cell:
a: 102.8Å b: 102.8Å c: 150.1Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.184 0.184 0.226
Expression system: Escherichia coli

Quick links

Citations

15 citation in other articles

Crystal structure of porcine mitochondrial NADP+-dependent isocitrate dehydrogenase complexed with Mn2+ and isocitrate. Insights into the enzyme mechanism.
Ceccarelli et al. (2002)
14 more

1 mention without citation

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