› 1xkd

X-ray diffraction
2.3Å resolution

Ternary complex of Isocitrate dehydrogenase from the hyperthermophile Aeropyrum pernix

Released:
DOI: 10.2210/pdb1xkd/pdb
PDB entry 1xkd coloured by chain, front view.
PDB entry 1xkd coloured by chain, side view.
PDB entry 1xkd coloured by chain, top view.
Source organism: Aeropyrum pernix K1
Primary publication:
Isocitrate dehydrogenase from the hyperthermophile Aeropyrum pernix: X-ray structure analysis of a ternary enzyme-substrate complex and thermal stability.
Karlström M, Stokke R, Steen IH, Birkeland NK, Ladenstein R
J Mol Biol 345 559-77 (2005)
PMID: 15581899

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-195486 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
isocitrate dehydrogenase (NADP(+)) Chains: A, B
Molecule details ›
Chains: A, B
Length: 435 amino acids
Theoretical weight: 47.98 KDa
Source organism: Aeropyrum pernix K1
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9YE81 (Residues: 1-432; Coverage: 100%)
Gene name: APE_0689.1
Sequence domains: Isocitrate/isopropylmalate dehydrogenase
Structure domains: Isopropylmalate Dehydrogenase

Ligands and Environments


Cofactor: Ligand NAP 2 x NAP
2 bound ligands:
Ligand CA 2 x CA
Ligand ICT 2 x ICT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I711
Spacegroup: P43212
Unit cell:
a: 107.575Å b: 107.575Å c: 171.045Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.227 0.226 0.248
Expression system: Escherichia coli

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Citations

2 review citations

Protein disulfides and protein disulfide oxidoreductases in hyperthermophiles.
Ladenstein et al. (2006)
1 more