2y43

X-ray diffraction
1.8Å resolution

Rad18 ubiquitin ligase RING domain structure

Released:
Source organism: Homo sapiens
Primary publication:
Symmetry and asymmetry of the RING-RING dimer of Rad18.
J Mol Biol 410 424-35 (2011)
PMID: 21549715

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:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-192586 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
E3 ubiquitin-protein ligase RAD18 Chains: A, B
Molecule details ›
Chains: A, B
Length: 99 amino acids
Theoretical weight: 11.38 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9NS91 (Residues: 1-99; Coverage: 20%)
Gene names: RAD18, RNF73
Sequence domains: Zinc finger, C3HC4 type (RING finger)
Structure domains: Zinc/RING finger domain, C3HC4 (zinc finger)

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: C2
Unit cell:
a: 104.646Å b: 29.357Å c: 69.736Å
α: 90° β: 125.05° γ: 90°
R-values:
R R work R free
0.177 0.175 0.223
Expression system: Escherichia coli BL21(DE3)