› 1o79

X-ray diffraction
2.8Å resolution

Structures of human oxidosqualene cyclase inhibitors bound to an homologous enzyme

Released:
DOI: 10.2210/pdb1o79/pdb
PDB entry 1o79 coloured by chain, front view.
PDB entry 1o79 coloured by chain, side view.
PDB entry 1o79 coloured by chain, top view.
Source organism: Alicyclobacillus acidocaldarius
Primary publication:
Binding structures and potencies of oxidosqualene cyclase inhibitors with the homologous squalene-hopene cyclase.
Lenhart A, Reinert DJ, Aebi JD, Dehmlow H, Morand OH, Schulz GE
J Med Chem 46 2083-92 (2003)
PMID: 12747780

Function and Biology Details

Reactions catalysed: 
Hopan-22-ol = squalene + H(2)O
Squalene = hop-22(29)-ene
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-152568 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Squalene--hopene cyclase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 631 amino acids
Theoretical weight: 71.65 KDa
Source organism: Alicyclobacillus acidocaldarius
Expression system: Escherichia coli K-12
UniProt:
  • Canonical: P33247 (Residues: 1-631; Coverage: 100%)
Gene names: Aaci_2443, shc
Sequence domains:
Structure domains: Glycosyltransferase

Ligands and Environments

2 bound ligands:
Ligand C8E 3 x C8E
Ligand R23 3 x R23
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200B
Spacegroup: P3221
Unit cell:
a: 141.289Å b: 141.289Å c: 245.397Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.239 0.239 0.273
Expression system: Escherichia coli K-12

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Citations

2 review citations

Cholesterol synthesis inhibitor U18666A and the role of sterol metabolism and trafficking in numerous pathophysiological processes.
Cenedella RJ. (2009)
1 more