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:
Structure analysis Details
Assembly composition:
hetero trimer (preferred)
Assembly name:
Protein farnesyltransferase complex and peptide (preferred)
PDBe Complex ID:
PDB-CPX-155934 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (4 distinct):
Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha
Molecule details ›
Chain: A
Length: 382 amino acids
Theoretical weight: 44.86 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: Protein prenyltransferase alpha subunit repeat
Structure domains: Protein prenylyltransferase
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%)
Sequence domains: Protein prenyltransferase alpha subunit repeat
Structure domains: Protein prenylyltransferase
Protein farnesyltransferase subunit beta
Molecule details ›
Chain: B
Length: 437 amino acids
Theoretical weight: 48.82 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: Prenyltransferase and squalene oxidase repeat
Structure domains: Glycosyltransferase
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%)
Sequence domains: Prenyltransferase and squalene oxidase repeat
Structure domains: Glycosyltransferase
