PDBe 3l2o

X-ray diffraction
2.8Å resolution

Structure-Based Mechanism of Dimerization-Dependent Ubiquitination by the SCFFbx4 Ubiquitin Ligase

Released:
Source organism: Homo sapiens
Primary publication:
Structural basis of dimerization-dependent ubiquitination by the SCF(Fbx4) ubiquitin ligase.
J. Biol. Chem. 285 13896-906 (2010)
PMID: 20181953

Function and Biology Details

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
hetero tetramer
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
S-phase kinase-associated protein 1 Chain: A
Molecule details ›
Chain: A
Length: 149 amino acids
Theoretical weight: 16.83 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P63208 (Residues: 1-69, 82-163; Coverage: 89%)
Gene names: EMC19, OCP2, SKP1, SKP1A, TCEB1L
Sequence domains:
Structure domains: Potassium Channel Kv1.1; Chain A
F-box only protein 4 Chain: B
Molecule details ›
Chain: B
Length: 312 amino acids
Theoretical weight: 35.85 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9UKT5 (Residues: 55-387; Coverage: 81%)
Gene names: FBX4, FBXO4
Sequence domains: F-box domain
Structure domains:

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X3A, NSLS BEAMLINE X29A
Spacegroup: P3121
Unit cell:
a: 92.194Å b: 92.194Å c: 148.068Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.252 0.249 0.295
Expression system: Escherichia coli BL21(DE3)