› 1qbq

X-ray diffraction
2.4Å resolution

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

Released:
DOI: 10.2210/pdb1qbq/pdb
PDB entry 1qbq coloured by chain, front view.
PDB entry 1qbq coloured by chain, side view.
PDB entry 1qbq coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Crystal structure of farnesyl protein transferase complexed with a CaaX peptide and farnesyl diphosphate analogue.
Strickland CL, Windsor WT, Syto R, Wang L, Bond R, Wu Z, Schwartz J, Le HV, Beese LS, Weber PC
Biochemistry 37 16601-11 (1998)
PMID: 9843427

Function and Biology Details

Reactions catalysed: 
Farnesyl diphosphate + protein-cysteine = S-farnesyl protein + diphosphate
Geranylgeranyl diphosphate + protein-cysteine = S-geranylgeranyl-protein + diphosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-162407 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
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
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
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:
Ligand ACT 1 x ACT
Ligand ZN 1 x ZN
Ligand HFP 1 x HFP
1 modified residue:
Ligand MSE 1 x MSE

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

Quick links

Citations

19 review citations

Structure, mechanism and function of prenyltransferases.
Liang et al. (2002)
18 more

9 mentions without citation

Protein Prenyltransferases and Their Inhibitors: Structural and Functional Characterization.
Marchwicka et al. (2022)
8 more