1tn6

X-ray diffraction
1.8Å resolution

Protein Farnesyltransferase Complexed with a Rap2a Peptide Substrate and a FPP Analog at 1.8A Resolution

Released:

Function and Biology Details

Reactions catalysed:
Geranylgeranyl diphosphate + protein-cysteine = S-geranylgeranyl-protein + diphosphate
Farnesyl diphosphate + protein-cysteine = S-farnesyl protein + diphosphate
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (4 distinct):
Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha Chain: A
Molecule details ›
Chain: A
Length: 382 amino acids
Theoretical weight: 44.86 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P49354 (Residues: 1-379; Coverage: 100%)
Gene name: FNTA
Structure domains: Protein prenylyltransferase
Protein farnesyltransferase subunit beta Chain: B
Molecule details ›
Chain: B
Length: 437 amino acids
Theoretical weight: 48.82 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P49356 (Residues: 1-437; Coverage: 100%)
Gene name: FNTB
Structure domains: Glycosyltransferase
peptide derived from the C-terminus of Rap2a Chain: C
Molecule details ›
Chain: C
Length: 11 amino acids
Theoretical weight: 1.13 KDa

Ligands and Environments

Carbohydrate polymer : NEW Components: GLC, FRU
3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-C
Spacegroup: P61
Unit cell:
a: 178.474Å b: 178.474Å c: 64.697Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.179 0.179 0.199
Expression system: Escherichia coli BL21(DE3)