3l82

X-ray diffraction
2.4Å resolution

X-ray Crystal structure of TRF1 and Fbx4 complex

Released:
Source organism: Homo sapiens
Primary publication:
Structural basis of selective ubiquitination of TRF1 by SCFFbx4.
Dev Cell 18 214-25 (2010)
PMID: 20159592

Function and Biology Details

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
hetero tetramer
PDBe Complex ID:
PDB-CPX-156972 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Telomeric repeat-binding factor 1 Chain: A
Molecule details ›
Chain: A
Length: 215 amino acids
Theoretical weight: 24.95 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P54274 (Residues: 58-268; Coverage: 48%)
Gene names: PIN2, TERF1, TRBF1, TRF, TRF1
Sequence domains: Telomere repeat binding factor (TRF)
Structure domains: Telomere repeat-binding factor, dimerisation domain
F-box only protein 4 Chain: B
Molecule details ›
Chain: B
Length: 227 amino acids
Theoretical weight: 25.98 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q9UKT5 (Residues: 162-387; Coverage: 58%)
Gene names: FBX4, FBXO4
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-D
Spacegroup: P43212
Unit cell:
a: 68.097Å b: 68.097Å c: 234.421Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.237 0.237 0.263
Expression system: Escherichia coli BL21