Structure analysis

Crystal Structure of Human Farnesyl Pyrophosphate Synthase (Y204F) Mutant Complexed with Mg, Risedronate and Isopentenyl Pyrophosphate

X-ray diffraction
1.96Å resolution
Source organism: Homo sapiens
Assembly composition:
homo dimer (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: homo dimer
Accessible surface area: 26208.05 Å2
Buried surface area: 6971.43 Å2
Dissociation area: 1,987.9 Å2
Dissociation energy (ΔGdiss): 22.24 kcal/mol
Dissociation entropy (TΔSdiss): 14.13 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-146902

Macromolecules

Chain: A
Length: 375 amino acids
Theoretical weight: 43.13 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P14324 (Residues: 67-419; Coverage: 84%)
Gene names: FDPS, FPS, KIAA1293
Pfam: Polyprenyl synthetase
InterPro:
CATH: Farnesyl Diphosphate Synthase

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