› 2huo

X-ray diffraction
2Å resolution

Crystal structure of mouse myo-inositol oxygenase in complex with substrate

Released:
DOI: 10.2210/pdb2huo/pdb
PDB entry 2huo coloured by chain, front view.
PDB entry 2huo coloured by chain, side view.
PDB entry 2huo coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Crystal structure of a substrate complex of myo-inositol oxygenase, a di-iron oxygenase with a key role in inositol metabolism.
Brown PM, Caradoc-Davies TT, Dickson JM, Cooper GJ, Loomes KM, Baker EN
Proc Natl Acad Sci U S A 103 15032-7 (2006)
PMID: 17012379

Function and Biology Details

Reaction catalysed: 
Myo-inositol + O(2) = D-glucuronate + H(2)O
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-193042 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Inositol oxygenase Chain: A
Molecule details ›
Chain: A
Length: 289 amino acids
Theoretical weight: 33.52 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9QXN5 (Residues: 1-285; Coverage: 100%)
Gene names: Aldrl6, Miox, Rsor
Sequence domains: Myo-inositol oxygenase

Ligands and Environments

4 bound ligands:
Ligand FE 2 x FE
Ligand OH 1 x OH
Ligand INS 1 x INS
Ligand FMT 1 x FMT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29, SSRL BEAMLINE BL9-2
Spacegroup: P212121
Unit cell:
a: 44.602Å b: 77.202Å c: 85.397Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.206 0.204 0.256
Expression system: Escherichia coli

Quick links

Citations

10 review citations

Dioxygen Activation by Nonheme Diiron Enzymes: Diverse Dioxygen Adducts, High-Valent Intermediates, and Related Model Complexes.
Jasniewski et al. (2018)
9 more

9 mentions without citation

Divergence and convergence in enzyme evolution.
Galperin et al. (2012)
8 more