PDBe 1uby

X-ray diffraction
2.4Å resolution

STRUCTURE OF FARNESYL PYROPHOSPHATE SYNTHETASE

Released:
Source organism: Gallus gallus
Primary publication:
Regulation of product chain length by isoprenyl diphosphate synthases.
Proc. Natl. Acad. Sci. U.S.A. 93 15018-23 (1996)
PMID: 8986756

Function and Biology Details

Reactions catalysed:
Geranyl diphosphate + isopentenyl diphosphate = diphosphate + (2E,6E)- farnesyl diphosphate. 
Dimethylallyl diphosphate + isopentenyl diphosphate = diphosphate + geranyl diphosphate. 
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Farnesyl pyrophosphate synthase Chain: A
Molecule details ›
Chain: A
Length: 367 amino acids
Theoretical weight: 42.01 KDa
Source organism: Gallus gallus
Expression system: Escherichia coli
UniProt:
  • Canonical: P08836 (Residues: 1-367; Coverage: 100%)
Gene name: FDPS
Sequence domains: Polyprenyl synthetase
Structure domains: Farnesyl Diphosphate Synthase

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: I4122
Unit cell:
a: 88.3Å b: 88.3Å c: 274.7Å
α: 90° β: 90° γ: 90°
Expression system: Escherichia coli