› 7cng

X-ray diffraction
3.49Å resolution

Structure of CDK5R1 bound FEM1B

Released:
DOI: 10.2210/pdb7cng/pdb
PDB entry 7cng coloured by chain, front view.
PDB entry 7cng coloured by chain, side view.
PDB entry 7cng coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Molecular basis for arginine C-terminal degron recognition by Cul2FEM1 E3 ligase.
Chen X, Liao S, Makaros Y, Guo Q, Zhu Z, Krizelman R, Dahan K, Tu X, Yao X, Koren I, Xu C
Nat Chem Biol 17 254-262 (2021)
PMID: 33398168

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-172188 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cyclin-dependent kinase 5 activator 1, p25; Protein fem-1 homolog B Chains: A, B
Molecule details ›
Chains: A, B
Length: 357 amino acids
Theoretical weight: 39.3 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'
UniProt:
  • Canonical: Q9UK73 (Residues: 1-337; Coverage: 54%)
  • Canonical: Q15078 (Residues: 298-307; Coverage: 3%)
Gene names: CDK5R, CDK5R1, F1AA, FEM1B, KIAA0396, NCK5A
Sequence domains: Ankyrin repeats (3 copies)

Ligands and Environments

1 bound ligand:
Ligand SO4 4 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL18U1
Spacegroup: P4212
Unit cell:
a: 126.812Å b: 126.812Å c: 144.489Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.225 0.22 0.267
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'

Quick links

Citations

1 review citation

Exploiting E3 ubiquitin ligases to reeducate the tumor microenvironment for cancer therapy.
Li et al. (2023)
14 other articles

2 mentions without citation

How the ends signal the end: Regulation by E3 ubiquitin ligases recognizing protein termini.
Sherpa et al. (2022)
1 more