› 3v66

X-ray diffraction
1.8Å resolution

HUMAN SQUALENE SYNTHASE IN COMPLEX WITH 2-(1-{2-[(4R,6S)-8-chloro-6-(2,3-dimethoxyphenyl)-4H,6H-pyrrolo[1,2-a][4,1]benzoxazepin-4-yl]acetyl}-4-piperidinyl)acetic acid

Released:
DOI: 10.2210/pdb3v66/pdb
PDB entry 3v66 coloured by chain, front view.
PDB entry 3v66 coloured by chain, side view.
PDB entry 3v66 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Discovery of novel tricyclic compounds as squalene synthase inhibitors.
Ichikawa M, Ohtsuka M, Ohki H, Haginoya N, Itoh M, Sugita K, Usui H, Suzuki M, Terayama K, Kanda A
Bioorg Med Chem 20 3072-93 (2012)
PMID: 22464687

Function and Biology Details

Reaction catalysed: 
(1a) 2 farnesyl diphosphate = diphosphate + presqualene diphosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153385 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Squalene synthase Chain: A
Molecule details ›
Chain: A
Length: 340 amino acids
Theoretical weight: 39.17 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P37268 (Residues: 31-370; Coverage: 82%)
Gene name: FDFT1
Sequence domains: Squalene/phytoene synthase
Structure domains: Farnesyl Diphosphate Synthase

Ligands and Environments

2 bound ligands:
Ligand PO4 1 x PO4
Ligand D3A 1 x D3A
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: C2
Unit cell:
a: 87.438Å b: 60.144Å c: 85.797Å
α: 90° β: 117.14° γ: 90°
R-values:
R R work R free
0.199 0.197 0.224
Expression system: Escherichia coli

Quick links

Citations

4 citation in other articles

Discovery of Potential Inhibitors of Squalene Synthase from Traditional Chinese Medicine Based on Virtual Screening and In Vitro Evaluation of Lipid-Lowering Effect.
Chen et al. (2018)
3 more

2 mentions without citation

Human isoprenoid synthase enzymes as therapeutic targets.
Park et al. (2014)
1 more