› 3m9u

X-ray diffraction
1.77Å resolution

Crystal structure of geranylgeranyl pyrophosphate synthase from lactobacillus brevis atcc 367

Released:
DOI: 10.2210/pdb3m9u/pdb
PDB entry 3m9u coloured by chain, front view.
PDB entry 3m9u coloured by chain, side view.
PDB entry 3m9u coloured by chain, top view.
Source organism: Levilactobacillus brevis ATCC 367
Entry authors: Patskovsky Y, Toro R, Rutter M, Sauder JM, Burley SK, Almo SC, New York Structural GenomiX Research Consortium (NYSGXRC), New York SGX Research Center for Structural Genomics (NYSGXRC)

Function and Biology Details

Reaction catalysed: 
Geranyl diphosphate + isopentenyl diphosphate = diphosphate + (2E,6E)-farnesyl diphosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assemblies composition:
homo tetramer
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-169978 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Farnesyl-diphosphate synthase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 309 amino acids
Theoretical weight: 33.34 KDa
Source organism: Levilactobacillus brevis ATCC 367
Expression system: Escherichia coli
UniProt:
  • Canonical: Q03RR4 (Residues: 3-300; Coverage: 99%)
Gene name: LVIS_0975
Sequence domains: Polyprenyl synthetase
Structure domains: Farnesyl Diphosphate Synthase

Ligands and Environments

1 bound ligand:
Ligand GOL 22 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P1
Unit cell:
a: 48.496Å b: 51.096Å c: 125.928Å
α: 95.47° β: 91.28° γ: 105.56°
R-values:
R R work R free
0.159 0.158 0.196
Expression system: Escherichia coli

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