› 3nt2

X-ray diffraction
2.3Å resolution

Crystal structure of myo-inositol dehydrogenase from Bacillus subtilis with bound cofactor

Released:
DOI: 10.2210/pdb3nt2/pdb
PDB entry 3nt2 coloured by chain, front view.
PDB entry 3nt2 coloured by chain, side view.
PDB entry 3nt2 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

Assemblies composition:
homo tetramer (preferred)
homo hexamer
Assembly name:
PDBe Complex ID:
PDB-CPX-150888 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Inositol 2-dehydrogenase/D-chiro-inositol 3-dehydrogenase Chains: A, B
Molecule details ›
Chains: A, B
Length: 344 amino acids
Theoretical weight: 38.39 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P26935 (Residues: 1-344; Coverage: 100%)
Gene names: BSU39700, E83G, idh, iolG
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand NAD 1 x NAD

Cofactor: Ligand NAI 1 x NAI
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CLSI BEAMLINE 08ID-1
Spacegroup: I213
Unit cell:
a: 184.368Å b: 184.368Å c: 184.368Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.242 0.24 0.286
Expression system: Escherichia coli BL21

Quick links

Citations

1 review citation

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

2 mentions without citation

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