› 1tyo

X-ray diffraction
2.15Å resolution

Isocitrate Dehydrogenase from the hyperthermophile Aeropyrum pernix in complex with etheno-NADP

Released:
DOI: 10.2210/pdb1tyo/pdb
PDB entry 1tyo coloured by chain, front view.
PDB entry 1tyo coloured by chain, side view.
PDB entry 1tyo coloured by chain, top view.
Source organism: Aeropyrum pernix
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
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

1 bound ligand:
Ligand ENP 1 x ENP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I711
Spacegroup: P43212
Unit cell:
a: 107.007Å b: 107.007Å c: 179.812Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.226 0.223 0.249
Expression system: Escherichia coli

Quick links

Citations

2 review citations

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

1 mention without citation

Functional relevance of dynamic properties of Dimeric NADP-dependent Isocitrate Dehydrogenases.
Vinekar et al. (2012)