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:
Protein farnesyltransferase complex (preferred)
PDBe Complex ID:
PDB-CPX-155932 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (3 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
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
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
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
UniProt:
- Canonical: P49356 (Residues: 1-437; Coverage: 100%)
Sequence domains: Prenyltransferase and squalene oxidase repeat
Structure domains: Glycosyltransferase
Ligands and Environments
Experiments and Validation Details
wwPDB Validation report is not available for this entry.
X-ray source:
RIGAKU RU200
Spacegroup:
P61
Expression system: Escherichia coli
