PDBe 2h0d

X-ray diffraction
2.5Å resolution

Structure of a Bmi-1-Ring1B Polycomb group ubiquitin ligase complex

Released:
Source organism: Homo sapiens
Primary publication:
Structure of a Bmi-1-Ring1B polycomb group ubiquitin ligase complex.
J. Biol. Chem. 281 20643-9 (2006)
PMID: 16714294

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:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Polycomb complex protein BMI-1 Chain: A
Molecule details ›
Chain: A
Length: 97 amino acids
Theoretical weight: 11.37 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P35226 (Residues: 5-101; Coverage: 30%)
Gene names: BMI1, PCGF4, RNF51
Sequence domains: Zinc finger, C3HC4 type (RING finger)
Structure domains: Zinc/RING finger domain, C3HC4 (zinc finger)
E3 ubiquitin-protein ligase RING2 Chain: B
Molecule details ›
Chain: B
Length: 100 amino acids
Theoretical weight: 11.48 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q99496 (Residues: 15-114; Coverage: 30%)
Gene names: BAP1, DING, HIPI3, RING1B, RNF2
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: NSLS BEAMLINE X25
Spacegroup: P63
Unit cell:
a: 120.514Å b: 120.514Å c: 27.209Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.211 0.21 0.244
Expression system: Escherichia coli BL21(DE3)