› 1tn6

X-ray diffraction
1.8Å resolution

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

Released:
DOI: 10.2210/pdb1tn6/pdb
PDB 1tn6 coloured by chain and viewed from the front.
PDB 1tn6 coloured by chain and viewed from the side.
PDB 1tn6 coloured by chain and viewed from the top.
Source organism: Homo sapiens
Primary publication:
Crystallographic analysis of CaaX prenyltransferases complexed with substrates defines rules of protein substrate selectivity.
Reid TS, Terry KL, Casey PJ, Beese LS
J. Mol. Biol. 343 417-33 (2004)
PMID: 15451670

Function and Biology Details

Reactions catalysed: 
Geranylgeranyl diphosphate + protein-cysteine = S-geranylgeranyl-protein + diphosphate
Farnesyl diphosphate + protein-cysteine = S-farnesyl protein + diphosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

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
Ligand GLC 1 x GLC
Ligand FRU 1 x FRU
3 bound ligands:
Ligand ACY 2 x ACY
Ligand FII 1 x FII
Ligand ZN 1 x ZN
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)

Quick links

Citations

28 review citations

Isoprenoids and protein prenylation: implications in the pathogenesis and therapeutic intervention of Alzheimer's disease.
Jeong et al. (2018)
27 more

7 mentions without citation

Structures of Cryptococcus neoformans protein farnesyltransferase reveal strategies for developing inhibitors that target fungal pathogens.
Hast et al. (2011)
6 more