PDBe 2ybf

X-ray diffraction
2Å resolution

Complex of Rad18 (Rad6 binding domain) with Rad6b

Released:
Source organism: Homo sapiens
Primary publication:
E3 ligase Rad18 promotes monoubiquitination rather than ubiquitin chain formation by E2 enzyme Rad6.
Proc. Natl. Acad. Sci. U.S.A. 108 5590-5 (2011)
PMID: 21422291

Function and Biology Details

Reactions catalysed:
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine
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:
Cellular component:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ubiquitin-conjugating enzyme E2 B Chain: A
Molecule details ›
Chain: A
Length: 152 amino acids
Theoretical weight: 17.33 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P63146 (Residues: 1-152; Coverage: 100%)
Gene names: RAD6B, UBE2B
Sequence domains: Ubiquitin-conjugating enzyme
Structure domains: Ubiquitin Conjugating Enzyme
E3 ubiquitin-protein ligase RAD18 Chain: B
Molecule details ›
Chain: B
Length: 27 amino acids
Theoretical weight: 3.22 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q9NS91 (Residues: 340-366; Coverage: 6%)
Gene names: RAD18, RNF73

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: P6522
Unit cell:
a: 58.21Å b: 58.21Å c: 167.07Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.201 0.199 0.242
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided