› 5vzt

X-ray diffraction
2.7Å resolution

Crystal structure of the Skp1-FBXO31 complex

Released:
DOI: 10.2210/pdb5vzt/pdb
PDB entry 5vzt coloured by chain, front view.
PDB entry 5vzt coloured by chain, side view.
PDB entry 5vzt coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis of the phosphorylation-independent recognition of cyclin D1 by the SCFFBXO31 ubiquitin ligase.
Li Y, Jin K, Bunker E, Zhang X, Luo X, Liu X, Hao B
Proc Natl Acad Sci U S A 115 319-324 (2018)
PMID: 29279382

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-159041 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
S-phase kinase-associated protein 1 Chains: A, C
Molecule details ›
Chains: A, C
Length: 149 amino acids
Theoretical weight: 16.83 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P63208 (Residues: 1-163; Coverage: 91%)
Gene names: EMC19, OCP2, SKP1, SKP1A, TCEB1L
Sequence domains:
Structure domains: Potassium Channel Kv1.1; Chain A
F-box only protein 31 Chains: B, D
Molecule details ›
Chains: B, D
Length: 488 amino acids
Theoretical weight: 55.73 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q5XUX0 (Residues: 66-539; Coverage: 88%)
Gene names: FBX14, FBX31, FBXO31, PP2386
Sequence domains:

Ligands and Environments

3 bound ligands:
Ligand ZN 2 x ZN
Ligand DTT 2 x DTT
Ligand PO4 8 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: C2
Unit cell:
a: 87.521Å b: 156.31Å c: 154.596Å
α: 90° β: 103.62° γ: 90°
R-values:
R R work R free
0.198 0.195 0.242
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

9 review citations

Structural insights into the functional diversity of the CDK-cyclin family.
Wood et al. (2018)
8 more

2 mentions without citation

Structural basis of the phosphorylation-independent recognition of cyclin D1 by the SCFFBXO31 ubiquitin ligase.
Li et al. (2018)
1 more