› 1sqc

X-ray diffraction
2.85Å resolution

SQUALENE-HOPENE-CYCLASE FROM ALICYCLOBACILLUS ACIDOCALDARIUS

Released:
DOI: 10.2210/pdb1sqc/pdb
PDB entry 1sqc coloured by chain, front view.
PDB entry 1sqc coloured by chain, side view.
PDB entry 1sqc coloured by chain, top view.
Source organism: Alicyclobacillus acidocaldarius
Primary publication:
Structure and function of a squalene cyclase.
Wendt KU, Poralla K, Schulz GE
Science 277 1811-5 (1997)
PMID: 9295270

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:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-152567 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Squalene--hopene cyclase Chain: A
Molecule details ›
Chain: A
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

1 bound ligand:
Ligand LDA 1 x LDA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P321
Unit cell:
a: 140.7Å b: 140.7Å c: 81.9Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.167 0.167 0.243
Expression system: Escherichia coli K-12

Quick links

Citations

59 review citations

Structure and function of fatty acid amide hydrolase.
McKinney et al. (2005)
58 more

9 mentions without citation

Multi-domain terpenoid cyclase architecture and prospects for proximity in bifunctional catalysis.
Chen et al. (2016)
8 more