PDBe 1qbq

X-ray diffraction
2.4Å resolution

STRUCTURE OF RAT FARNESYL PROTEIN TRANSFERASE COMPLEXED WITH A CVIM PEPTIDE AND ALPHA-HYDROXYFARNESYLPHOSPHONIC ACID.

Released:

Function and Biology Details

Reactions catalysed:
Farnesyl diphosphate + protein-cysteine = S-farnesyl protein + diphosphate
Geranylgeranyl diphosphate + protein-cysteine = S-geranylgeranyl-protein + diphosphate

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Protein farnesyltransferase subunit beta Chain: B
Molecule details ›
Chain: B
Length: 437 amino acids
Theoretical weight: 48.72 KDa
Source organism: Rattus norvegicus
Expression system: Not provided
UniProt:
  • Canonical: Q02293 (Residues: 1-437; Coverage: 100%)
Gene name: Fntb
Sequence domains: Prenyltransferase and squalene oxidase repeat
Structure domains: Glycosyltransferase
Protein farnesyltransferase/ geranylgeranyltransferase type-1 subunit alpha Chain: A
Molecule details ›
Chain: A
Length: 333 amino acids
Theoretical weight: 39.76 KDa
Source organism: Rattus norvegicus
Expression system: Not provided
UniProt:
  • Canonical: Q04631 (Residues: 45-377; Coverage: 88%)
Gene name: Fnta
Sequence domains: Protein prenyltransferase alpha subunit repeat
Structure domains: Protein prenylyltransferase
ACETYL-CYS-VAL-ILE-SELENOMET-COOH PEPTIDE Chain: P
Molecule details ›
Chain: P
Length: 5 amino acids
Theoretical weight: 538 Da

Ligands and Environments

3 bound ligands:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P61
Unit cell:
a: 174.132Å b: 174.132Å c: 69.705Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.218 0.218 0.292
Expression system: Not provided