PDBe 3l11

X-ray diffraction
2.12Å resolution

Crystal Structure of the Ring Domain of RNF168

Released:

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:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
E3 ubiquitin-protein ligase RNF168 Chain: A
Molecule details ›
Chain: A
Length: 115 amino acids
Theoretical weight: 13.13 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8IYW5 (Residues: 1-113; Coverage: 20%)
Gene name: RNF168
Sequence domains: Prokaryotic RING finger family 4
Structure domains: Zinc/RING finger domain, C3HC4 (zinc finger)

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E SUPERBRIGHT
Spacegroup: P43212
Unit cell:
a: 49.706Å b: 49.706Å c: 110.149Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.187 0.215
Expression system: Escherichia coli BL21(DE3)