› 1n95

X-ray diffraction
2.3Å resolution

Aryl Tetrahydrophyridine Inhbitors of Farnesyltranferase: Glycine, Phenylalanine and Histidine Derivatives

Released:
DOI: 10.2210/pdb1n95/pdb
PDB entry 1n95 coloured by chain, front view.
PDB entry 1n95 coloured by chain, side view.
PDB entry 1n95 coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Aryl tetrahydropyridine inhibitors of farnesyltransferase: glycine, phenylalanine and histidine derivatives.
Gwaltney SL, O'Connor SJ, Nelson LT, Sullivan GM, Imade H, Wang W, Hasvold L, Li Q, Cohen J, Gu WZ, Tahir SK, Bauch J, Marsh K, Ng SC, Frost DJ, Zhang H, Muchmore S, Jakob CG, Stoll V, Hutchins C, Rosenberg SH, Sham HL
Bioorg Med Chem Lett 13 1359-62 (2003)
PMID: 12657282

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 dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-169704 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha Chain: A
Molecule details ›
Chain: A
Length: 315 amino acids
Theoretical weight: 38.02 KDa
Source organism: Rattus norvegicus
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: Q04631 (Residues: 55-369; Coverage: 84%)
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: 402 amino acids
Theoretical weight: 44.98 KDa
Source organism: Rattus norvegicus
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: Q02293 (Residues: 22-423; Coverage: 92%)
Gene name: Fntb
Sequence domains: Prenyltransferase and squalene oxidase repeat
Structure domains: Glycosyltransferase

Ligands and Environments

3 bound ligands:
Ligand ZN 1 x ZN
Ligand HFP 1 x HFP
Ligand FTH 1 x FTH
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P61
Unit cell:
a: 171.126Å b: 171.126Å c: 69.404Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.337 0.337 0.358
Expression system: Spodoptera frugiperda

Quick links

Citations

1 review citation

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

2 mentions without citation

Virtual lead identification of farnesyltransferase inhibitors based on ligand and structure-based pharmacophore techniques.
Al-Balas et al. (2013)
1 more