1nl4

X-ray diffraction
2.7Å resolution

Crystal Structure of Rat Farnesyl Transferase in Complex With A Potent Biphenyl Inhibitor

Released:

Function and Biology Details

Reactions catalysed:
Geranylgeranyl diphosphate + protein-cysteine = S-geranylgeranyl-protein + diphosphate
Farnesyl diphosphate + protein-cysteine = S-farnesyl protein + diphosphate
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
Non-polymer only dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha Chain: A
Molecule details ›
Chain: A
Length: 312 amino acids
Theoretical weight: 37.63 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q04631 (Residues: 55-366; Coverage: 83%)
Gene name: Fnta
Sequence domains: Protein prenyltransferase alpha subunit repeat
Structure domains: Protein prenylyltransferase
Protein farnesyltransferase subunit beta Chain: B
Molecule details ›
Chain: B
Length: 401 amino acids
Theoretical weight: 44.88 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q02293 (Residues: 23-423; Coverage: 92%)
Gene name: Fntb
Sequence domains: Prenyltransferase and squalene oxidase repeat
Structure domains: Glycosyltransferase

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P61
Unit cell:
a: 168.62Å b: 168.62Å c: 69.123Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.231 0.229 0.283
Expression system: Escherichia coli