› 1d8d

X-ray diffraction
2Å resolution

CO-CRYSTAL STRUCTURE OF RAT PROTEIN FARNESYLTRANSFERASE COMPLEXED WITH A K-RAS4B PEPTIDE SUBSTRATE AND FPP ANALOG AT 2.0A RESOLUTION

Released:
DOI: 10.2210/pdb1d8d/pdb
PDB entry 1d8d coloured by chain, front view.
PDB entry 1d8d coloured by chain, side view.
PDB entry 1d8d coloured by chain, top view.
Source organisms:
Primary publication:
The basis for K-Ras4B binding specificity to protein farnesyltransferase revealed by 2 A resolution ternary complex structures.
Long SB, Casey PJ, Beese LS
Structure 8 209-22 (2000)
PMID: 10673434

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: P
Molecule details ›
Chain: P
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

3 bound ligands:
Ligand ZN 1 x ZN
Ligand ACT 4 x ACT
Ligand FII 1 x FII
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P61
Unit cell:
a: 170.919Å b: 170.919Å c: 69.284Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.171 0.164 0.2
Expression systems:
  • Spodoptera frugiperda
  • Not provided

Quick links

Citations

8 review citations

Thematic review series: lipid posttranslational modifications. Structural biology of protein farnesyltransferase and geranylgeranyltransferase type I.
Lane et al. (2006)
7 more

20 mentions without citation

Protein prenylation: enzymes, therapeutics, and biotechnology applications.
Palsuledesai et al. (2015)
19 more