› 1tn8

X-ray diffraction
2.25Å resolution

Protein Farnesyltransferase Complexed with a H-Ras Peptide Substrate and a FPP Analog at 2.25A Resolution

Released:
DOI: 10.2210/pdb1tn8/pdb
PDB entry 1tn8 coloured by chain, front view.
PDB entry 1tn8 coloured by chain, side view.
PDB entry 1tn8 coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Crystallographic analysis of CaaX prenyltransferases complexed with substrates defines rules of protein substrate selectivity.
Reid TS, Terry KL, Casey PJ, Beese LS
J Mol Biol 343 417-33 (2004)
PMID: 15451670

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-162469 (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
peptide derived from the C-terminus of H-Ras Chain: C
Molecule details ›
Chain: C
Length: 5 amino acids
Theoretical weight: 478 Da

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P61
Unit cell:
a: 171.147Å b: 171.147Å c: 69.326Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.193 0.193 0.218
Expression system: Spodoptera frugiperda

Quick links

Citations

35 review citations

Targeting the Raf-MEK-ERK mitogen-activated protein kinase cascade for the treatment of cancer.
Roberts et al. (2007)
34 more

5 mentions without citation

Isoprenoids and protein prenylation: implications in the pathogenesis and therapeutic intervention of Alzheimer's disease.
Jeong et al. (2018)
4 more