› 3wek

X-ray diffraction
1.85Å resolution

Crystal structure of the human squalene synthase F288L mutant in complex with presqualene pyrophosphate

Released:
DOI: 10.2210/pdb3wek/pdb
PDB entry 3wek coloured by chain, front view.
PDB entry 3wek coloured by chain, side view.
PDB entry 3wek coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural insights into the catalytic mechanism of human squalene synthase.
Liu CI, Jeng WY, Chang WJ, Shih MF, Ko TP, Wang AH
Acta Crystallogr D Biol Crystallogr 70 231-41 (2014)
PMID: 24531458

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: 343 amino acids
Theoretical weight: 39.41 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 MG 1 x MG
Ligand PS7 1 x PS7
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC BEAMLINE BL13B1
Spacegroup: P21212
Unit cell:
a: 94.192Å b: 106.502Å c: 32.988Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.227 0.225 0.257
Expression system: Escherichia coli

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Citations

1 review citation

Unveiling the Therapeutic Potential of Squalene Synthase: Deciphering Its Biochemical Mechanism, Disease Implications, and Intriguing Ties to Ferroptosis.
Picón et al. (2023)
21 other articles

1 mention without citation

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