1ld8

X-ray diffraction
1.8Å resolution

Function and Biology Details

Reactions catalysed:
Farnesyl diphosphate + protein-cysteine = S-farnesyl protein + diphosphate
Geranylgeranyl diphosphate + protein-cysteine = S-geranylgeranyl-protein + diphosphate

Structure analysis Details

Assembly composition:
Non-polymer only dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (3 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
UniProt:
  • Canonical: P49354 (Residues: 1-379; 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: 48.82 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P49356 (Residues: 1-437; Coverage: 100%)
Gene name: FNTB
Sequence domains: Prenyltransferase and squalene oxidase repeat
Structure domains: Glycosyltransferase

Ligands and Environments

Carbohydrate polymer : NEW Components: GLC, FRU
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P61
Unit cell:
a: 178.134Å b: 178.134Å c: 64.461Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.184 0.184 0.202
Expression system: Escherichia coli