› 1uby

X-ray diffraction
2.4Å resolution

STRUCTURE OF FARNESYL PYROPHOSPHATE SYNTHETASE

Released:
DOI: 10.2210/pdb1uby/pdb
PDB entry 1uby coloured by chain, front view.
PDB entry 1uby coloured by chain, side view.
PDB entry 1uby coloured by chain, top view.
Source organism: Gallus gallus
Primary publication:
Regulation of product chain length by isoprenyl diphosphate synthases.
Tarshis LC, Proteau PJ, Kellogg BA, Sacchettini JC, Poulter CD
Proc Natl Acad Sci U S A 93 15018-23 (1996)
PMID: 8986756

Function and Biology Details

Reactions catalysed: 
Prenyl diphosphate + isopentenyl diphosphate = diphosphate + geranyl diphosphate
Geranyl diphosphate + isopentenyl diphosphate = diphosphate + (2E,6E)-farnesyl diphosphate
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-140391 (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:
Ligand MG 2 x MG
Ligand DMA 1 x DMA
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

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Citations

38 review citations

Monoterpene and sesquiterpene synthases and the origin of terpene skeletal diversity in plants.
Degenhardt et al. (2009)
37 more

10 mentions without citation

Regulation of product chain length by isoprenyl diphosphate synthases.
Tarshis et al. (1996)
9 more