› 1kzo

X-ray diffraction
2.2Å resolution

PROTEIN FARNESYLTRANSFERASE COMPLEXED WITH FARNESYLATED K-RAS4B PEPTIDE PRODUCT AND FARNESYL DIPHOSPHATE SUBSTRATE BOUND SIMULTANEOUSLY

Released:
DOI: 10.2210/pdb1kzo/pdb
PDB entry 1kzo coloured by chain, front view.
PDB entry 1kzo coloured by chain, side view.
PDB entry 1kzo coloured by chain, top view.
Source organisms:
Primary publication:
Reaction path of protein farnesyltransferase at atomic resolution.
Long SB, Casey PJ, Beese LS
Nature 419 645-50 (2002)
PMID: 12374986

Function and Biology Details

Reactions catalysed: 
Farnesyl diphosphate + protein-cysteine = S-farnesyl protein + diphosphate
Geranylgeranyl diphosphate + protein-cysteine = S-geranylgeranyl-protein + diphosphate
GTP + H(2)O = GDP + phosphate
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-134020 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha Chain: A
Molecule details ›
Chain: A
Length: 377 amino acids
Theoretical weight: 44.1 KDa
Source organism: Rattus norvegicus
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: Q04631 (Residues: 1-377; Coverage: 100%)
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: Spodoptera frugiperda
UniProt:
  • Canonical: Q02293 (Residues: 1-437; Coverage: 100%)
Gene name: Fntb
Sequence domains: Prenyltransferase and squalene oxidase repeat
Structure domains: Glycosyltransferase
GTPase KRas, N-terminally processed Chain: C
Molecule details ›
Chain: C
Length: 11 amino acids
Theoretical weight: 1.3 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P01116 (Residues: 185-189; Coverage: 3%)
Gene names: KRAS, KRAS2, RASK2

Ligands and Environments

4 bound ligands:
Ligand ZN 1 x ZN
Ligand FPP 1 x FPP
Ligand ACY 1 x ACY
Ligand FAR 1 x FAR
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: P61
Unit cell:
a: 171.199Å b: 171.199Å c: 69.444Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.162 0.159 0.204
Expression systems:
  • Spodoptera frugiperda
  • Not provided

Quick links

Citations

30 review citations

Protein prenylation: unique fats make their mark on biology.
Wang et al. (2016)
29 more

8 mentions without citation

Prenyltransferase Inhibitors: Treating Human Ailments from Cancer to Parasitic Infections.
Ochocki et al. (2013)
7 more