› 3qvx

X-ray diffraction
1.9Å resolution

L-myo-inositol 1-phosphate synthase from Archaeoglobus fulgidus mutant K367A

Released:
DOI: 10.2210/pdb3qvx/pdb
PDB entry 3qvx coloured by chain, front view.
PDB entry 3qvx coloured by chain, side view.
PDB entry 3qvx coloured by chain, top view.
Source organism: Archaeoglobus fulgidus
Primary publication:
Crystal structure of a trapped catalytic intermediate suggests that forced atomic proximity drives the catalysis of mIPS.
Neelon K, Roberts MF, Stec B
Biophys J 101 2816-24 (2011)
PMID: 22261071

Function and Biology Details

Reaction catalysed: 
D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-128030 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
inositol-3-phosphate synthase Chain: A
Molecule details ›
Chain: A
Length: 392 amino acids
Theoretical weight: 43.71 KDa
Source organism: Archaeoglobus fulgidus
Expression system: Escherichia coli
UniProt:
  • Canonical: O28480 (Residues: 1-392; Coverage: 100%)
Gene name: AF_1794
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand NAD 1 x NAD
5 bound ligands:
Ligand PO4 1 x PO4
Ligand SO4 2 x SO4
Ligand GOL 4 x GOL
Ligand PG4 1 x PG4
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: I222
Unit cell:
a: 82.07Å b: 89.28Å c: 104.97Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.177 0.175 0.229
Expression system: Escherichia coli

Quick links

Citations

6 citation in other articles

Phosphorylation regulates myo-inositol-3-phosphate synthase: a novel regulatory mechanism of inositol biosynthesis.
Deranieh et al. (2013)
5 more

1 mention without citation

Crystal structure of a trapped catalytic intermediate suggests that forced atomic proximity drives the catalysis of mIPS.
Neelon et al. (2011)