› 2qis

X-ray diffraction
1.8Å resolution

Crystal structure of human farnesyl pyrophosphate synthase T210S mutant bound to risedronate

Released:
DOI: 10.2210/pdb2qis/pdb
PDB entry 2qis coloured by chain, front view.
PDB entry 2qis coloured by chain, side view.
PDB entry 2qis coloured by chain, top view.
Source organism: Homo sapiens
Entry authors: Kavanagh KL, Dunford JE, Hozjan V, Evdokimov A, Gileadi O, von Delft F, Weigelt J, Arrowsmith CH, Sundstrom M, Edwards A, Oppermann U, Structural Genomics Consortium (SGC)

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146902 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Farnesyl pyrophosphate synthase Chain: A
Molecule details ›
Chain: A
Length: 374 amino acids
Theoretical weight: 43 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P14324 (Residues: 67-419; Coverage: 84%)
Gene names: FDPS, FPS, KIAA1293
Sequence domains: Polyprenyl synthetase
Structure domains: Farnesyl Diphosphate Synthase

Ligands and Environments

2 bound ligands:
Ligand MG 3 x MG
Ligand RIS 1 x RIS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P41212
Unit cell:
a: 111.47Å b: 111.47Å c: 67.603Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.179 0.178 0.206
Expression system: Escherichia coli BL21(DE3)

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