› 1la2

X-ray diffraction
2.65Å resolution

Structural analysis of Saccharomyces cerevisiae myo-inositol phosphate synthase

Released:
DOI: 10.2210/pdb1la2/pdb
PDB entry 1la2 coloured by chain, front view.
PDB entry 1la2 coloured by chain, side view.
PDB entry 1la2 coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Structural analysis of Saccharomyces cerevisiae myo-inositol phosphate synthase.
Kniewel R, Buglino JA, Shen V, Chadha T, Beckwith A, Lima CD
J Struct Funct Genomics 2 129-34 (2002)
PMID: 12836703

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146022 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Inositol-3-phosphate synthase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 533 amino acids
Theoretical weight: 60.18 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: P11986 (Residues: 1-533; Coverage: 100%)
Gene names: INO1, J0610, YJL153C
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand NAD 4 x NAD
No bound ligands
1 modified residue:
Ligand MSE 40 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X9A
Spacegroup: P21212
Unit cell:
a: 155.693Å b: 187.346Å c: 98.954Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.224 0.224 0.28
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Biosynthesis of aminocyclitol-aminoglycoside antibiotics and related compounds.
Flatt et al. (2007)
1 more

1 mention without citation

High-throughput computational and experimental techniques in structural genomics.
Chance et al. (2004)