› 1ump

X-ray diffraction
2.13Å resolution

GEOMETRY OF TRITERPENE CONVERSION TO PENTACARBOCYCLIC HOPENE

Released:
DOI: 10.2210/pdb1ump/pdb
PDB entry 1ump coloured by chain, front view.
PDB entry 1ump coloured by chain, side view.
PDB entry 1ump coloured by chain, top view.
Source organism: Alicyclobacillus acidocaldarius
Primary publication:
Conversion of squalene to the pentacarbocyclic hopene.
Reinert DJ, Balliano G, Schulz GE
Chem Biol 11 121-6 (2004)
PMID: 15113001

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 5 x C8E
Ligand SQA 3 x SQA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P3221
Unit cell:
a: 139.144Å b: 139.144Å c: 240.699Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.187 0.186 0.228
Expression system: Escherichia coli K-12

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Citations

18 review citations

Structural and Chemical Biology of Terpenoid Cyclases.
Christianson DW. (2017)
17 more

11 mentions without citation

Squalene-hopene cyclases.
Siedenburg et al. (2011)
10 more