› 6g32

X-ray diffraction
3.28Å resolution

Crystal structure of human geranylgeranyl diphosphate synthase mutant D188Y

Released:
DOI: 10.2210/pdb6g32/pdb
PDB 6g32 coloured by chain and viewed from the front.
PDB 6g32 coloured by chain and viewed from the side.
PDB 6g32 coloured by chain and viewed from the top.
Source organism: Homo sapiens
Primary publication:
Reduced Activity of GGPPS Mutant is Involved in Bisphosphonates-Induced Atypical Fractures.
Lisnyansky M, Kapelushnik N, Ben-Bassat A, Marom M, Loewenstein A, Khananshvili D, Giladi M, Haitin Y
Mol. Pharmacol. (2018)
PMID: 30275041

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo hexamer (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: 307 amino acids
Theoretical weight: 35.48 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O95749 (Residues: 1-300; Coverage: 100%)
Gene name: GGPS1
Sequence domains: Polyprenyl synthetase
Structure domains: Farnesyl Diphosphate Synthase

Ligands and Environments

1 bound ligand:
Ligand GOL 6 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID30B
Spacegroup: P43212
Unit cell:
a: 148.54Å b: 148.54Å c: 268.23Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.208 0.206 0.258
Expression system: Escherichia coli

Quick links

Citations

2 review citations

The catalytic and structural basis of archaeal glycerophospholipid biosynthesis.
de Kok et al. (2022)
1 more