› 1iso

X-ray diffraction
1.9Å resolution

ISOCITRATE DEHYDROGENASE: STRUCTURE OF AN ENGINEERED NADP+--> NAD+ SPECIFICITY-REVERSAL MUTANT

Released:
DOI: 10.2210/pdb1iso/pdb
PDB entry 1iso coloured by chain, front view.
PDB entry 1iso coloured by chain, side view.
PDB entry 1iso coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Determinants of cofactor specificity in isocitrate dehydrogenase: structure of an engineered NADP+ --> NAD+ specificity-reversal mutant.
Hurley JH, Chen R, Dean AM
Biochemistry 35 5670-8 (1996)
PMID: 8639526

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: 45.7 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


Cofactor: Ligand NAD 1 x NAD
1 bound ligand:
Ligand SO4 3 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P43212
Unit cell:
a: 102.4Å b: 102.4Å c: 150.6Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.186 0.186 0.218
Expression system: Not provided

Quick links

Citations

7 review citations

Molecular-functional studies of adaptive genetic variation in prokaryotes and eukaryotes.
Watt et al. (2000)
6 more

4 mentions without citation

Reducing the computational complexity of protein folding via fragment folding and assembly.
Haspel et al. (2003)
3 more