› 1s64

X-ray diffraction
2.55Å resolution

Rat protein geranylgeranyltransferase type-I complexed with L-778,123 and a sulfate anion

Released:
DOI: 10.2210/pdb1s64/pdb
PDB entry 1s64 coloured by chain, front view.
PDB entry 1s64 coloured by chain, side view.
PDB entry 1s64 coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Crystallographic analysis reveals that anticancer clinical candidate L-778,123 inhibits protein farnesyltransferase and geranylgeranyltransferase-I by different binding modes.
Reid TS, Long SB, Beese LS
Biochemistry 43 9000-8 (2004)
PMID: 15248757

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-156827 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha Chains: A, C, E, G, I, K
Molecule details ›
Chains: A, C, E, G, I, K
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
Geranylgeranyl transferase type-1 subunit beta Chains: B, D, F, H, J, L
Molecule details ›
Chains: B, D, F, H, J, L
Length: 377 amino acids
Theoretical weight: 42.47 KDa
Source organism: Rattus norvegicus
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P53610 (Residues: 1-377; Coverage: 100%)
Gene name: Pggt1b
Sequence domains: Prenyltransferase and squalene oxidase repeat
Structure domains: Glycosyltransferase

Ligands and Environments

5 bound ligands:
Ligand ZN 6 x ZN
Ligand SO4 6 x SO4
Ligand 778 6 x 778
Ligand MES 6 x MES
Ligand CL 9 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-C
Spacegroup: C2
Unit cell:
a: 271.153Å b: 268.681Å c: 184.622Å
α: 90° β: 131.55° γ: 90°
R-values:
R R work R free
0.192 0.192 0.213
Expression system: Spodoptera frugiperda

Quick links

Citations

11 review citations

Nitrile-containing pharmaceuticals: efficacious roles of the nitrile pharmacophore.
Fleming et al. (2010)
10 more

2 mentions without citation

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