› 4ppe

X-ray diffraction
2Å resolution

Function and Biology Details

Reaction catalysed: 
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-160231 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
E3 ubiquitin-protein ligase RNF4 Chains: A, B
Molecule details ›
Chains: A, B
Length: 76 amino acids
Theoretical weight: 8.27 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P78317 (Residues: 120-190; Coverage: 37%)
Gene names: RES4-26, RNF4, SNURF
Sequence domains: Ring finger domain
Structure domains: Zinc/RING finger domain, C3HC4 (zinc finger)

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 12.3.1
Spacegroup: P21212
Unit cell:
a: 59.938Å b: 86.987Å c: 22.869Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.232 0.23 0.28
Expression system: Escherichia coli

Quick links

Citations

14 review citations

Spatiotemporal regulation of posttranslational modifications in the DNA damage response.
Dantuma et al. (2016)
13 more

7 mentions without citation

The BRCA1 Ubiquitin ligase function sets a new trend for remodelling in DNA repair.
Densham et al. (2017)
6 more