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X-ray diffraction
1.85Å resolution

Function and Biology Details

Reaction catalysed: 
All-trans-heptaprenyl diphosphate + sn-glycerol 1-phosphate = diphosphate + sn-3-O-(all-trans-heptaprenyl)glycerol 1-phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-128596 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Heptaprenylglyceryl phosphate synthase Chains: A, B
Molecule details ›
Chains: A, B
Length: 240 amino acids
Theoretical weight: 26.47 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
  • Canonical: O34790 (Residues: 2-228; Coverage: 100%)
Gene names: BSU06600, pcrB, yerE
Sequence domains: PcrB family
Structure domains: FMN-linked oxidoreductases

Ligands and Environments

1 bound ligand:
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 32-ID
Spacegroup: P32
Unit cell:
a: 86.46Å b: 86.46Å c: 54.141Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.202 0.202 0.258
Expression system: Escherichia coli

Quick links

Citations

23 review citations

Regulation of fatty acid metabolism in bacteria.
Fujita et al. (2007)
22 more

2 mentions without citation

High-throughput computational and experimental techniques in structural genomics.
Chance et al. (2004)
1 more