› 3mz0

X-ray diffraction
1.54Å resolution

Crystal structure of apo myo-inositol dehydrogenase from Bacillus subtilis

Released:
DOI: 10.2210/pdb3mz0/pdb
PDB entry 3mz0 coloured by chain, front view.
PDB entry 3mz0 coloured by chain, side view.
PDB entry 3mz0 coloured by chain, top view.
Source organism: Bacillus subtilis
Primary publication:
Structural investigation of myo-inositol dehydrogenase from Bacillus subtilis: implications for catalytic mechanism and inositol dehydrogenase subfamily classification.
van Straaten KE, Zheng H, Palmer DR, Sanders DA
Biochem J 432 237-47 (2010)
PMID: 20809899

Function and Biology Details

Reactions catalysed: 
Myo-inositol + NAD(+) = 2,4,6/3,5-pentahydroxycyclohexanone + NADH
1D-chiro-inositol + NAD(+) = 2D-2,3,5/4,6-pentahydroxycyclohexanone + NADH
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150888 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Inositol 2-dehydrogenase/D-chiro-inositol 3-dehydrogenase Chain: A
Molecule details ›
Chain: A
Length: 344 amino acids
Theoretical weight: 38.68 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P26935 (Residues: 1-344; Coverage: 100%)
Gene names: BSU39700, E83G, idh, iolG
Sequence domains:
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand PGE 2 x PGE
Ligand GOL 1 x GOL
Ligand CL 4 x CL
Ligand MG 1 x MG
1 modified residue:
Ligand MSE 6 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: CLSI BEAMLINE 08ID-1
Spacegroup: I222
Unit cell:
a: 52.207Å b: 120.054Å c: 129.254Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.176 0.175 0.194
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Structure and function of aldopentose catabolism enzymes involved in oxidative non-phosphorylative pathways.
Ren et al. (2022)
9 other articles

1 mention without citation

Structural and functional features of the NAD(P) dependent Gfo/Idh/MocA protein family oxidoreductases.
Taberman et al. (2016)