› 3v7d

X-ray diffraction
2.31Å resolution

Crystal Structure of ScSkp1-ScCdc4-pSic1 peptide complex

Released:
DOI: 10.2210/pdb3v7d/pdb
PDB entry 3v7d coloured by chain, front view.
PDB entry 3v7d coloured by chain, side view.
PDB entry 3v7d coloured by chain, top view.
Source organism: Saccharomyces cerevisiae S288C
Primary publication:
Composite low affinity interactions dictate recognition of the cyclin-dependent kinase inhibitor Sic1 by the SCFCdc4 ubiquitin ligase.
Tang X, Orlicky S, Mittag T, Csizmok V, Pawson T, Forman-Kay JD, Sicheri F, Tyers M
Proc Natl Acad Sci U S A 109 3287-92 (2012)
PMID: 22328159

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assemblies composition:
hetero trimer (preferred)
hetero dimer
PDBe Complex ID:
PDB-CPX-139780 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Suppressor of kinetochore protein 1 Chains: A, C
Molecule details ›
Chains: A, C
Length: 169 amino acids
Theoretical weight: 19.5 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
  • Canonical: P52286 (Residues: 1-194; Coverage: 86%)
Gene names: CBF3D, D9798.14, SKP1, YDR328C
Sequence domains:
Structure domains: Potassium Channel Kv1.1; Chain A
Cell division control protein 4 Chains: B, D
Molecule details ›
Chains: B, D
Length: 464 amino acids
Theoretical weight: 52.86 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
  • Canonical: P07834 (Residues: 263-744; Coverage: 59%)
Gene names: CDC4, YFL009W
Sequence domains:
Structure domains:
Protein SIC1 Chain: E
Molecule details ›
Chain: E
Length: 19 amino acids
Theoretical weight: 2.32 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Not provided
UniProt:
  • Canonical: P38634 (Residues: 67-85; Coverage: 7%)
Gene names: L9449.8, SDB25, SIC1, YLR079W

Ligands and Environments

No bound ligands
1 modified residue:
Ligand SEP 3 x SEP

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-C
Spacegroup: P32
Unit cell:
a: 107.292Å b: 107.292Å c: 166.679Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.197 0.196 0.221
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

8 review citations

Mechanisms and function of substrate recruitment by F-box proteins.
Skaar et al. (2013)
7 more

5 mentions without citation

NMR contributions to structural dynamics studies of intrinsically disordered proteins.
Konrat R. (2014)
4 more