› 2q80

X-ray diffraction
2.7Å resolution

Crystal structure of human geranylgeranyl pyrophosphate synthase bound to GGPP

Released:
DOI: 10.2210/pdb2q80/pdb
PDB entry 2q80 coloured by chain, front view.
PDB entry 2q80 coloured by chain, side view.
PDB entry 2q80 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The crystal structure of human geranylgeranyl pyrophosphate synthase reveals a novel hexameric arrangement and inhibitory product binding.
Kavanagh KL, Dunford JE, Bunkoczi G, Russell RGG, Oppermann U
J Biol Chem 281 22004-22012 (2006)
PMID: 16698791

Function and Biology Details

Reactions catalysed: 
Prenyl diphosphate + isopentenyl diphosphate = diphosphate + geranyl diphosphate
Geranyl diphosphate + isopentenyl diphosphate = diphosphate + (2E,6E)-farnesyl diphosphate
(2E,6E)-farnesyl diphosphate + isopentenyl diphosphate = diphosphate + geranylgeranyl diphosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132011 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Geranylgeranyl pyrophosphate synthase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 301 amino acids
Theoretical weight: 35 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O95749 (Residues: 1-300; Coverage: 100%)
Gene name: GGPS1
Sequence domains: Polyprenyl synthetase
Structure domains: Farnesyl Diphosphate Synthase

Ligands and Environments

2 bound ligands:
Ligand MG 12 x MG
Ligand GRG 6 x GRG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P41212
Unit cell:
a: 141.248Å b: 141.248Å c: 211.705Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.204 0.202 0.253
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

26 review citations

Mechanisms of action of bisphosphonates: similarities and differences and their potential influence on clinical efficacy.
Russell et al. (2008)
25 more

11 mentions without citation

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