2ckl

X-ray diffraction
2Å resolution

Ring1b-Bmi1 E3 catalytic domain structure

Released:
Model geometry
Fit model/data

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:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-150612 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Polycomb complex protein BMI-1 Chain: A
Molecule details ›
Chain: A
Length: 108 amino acids
Theoretical weight: 12.53 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P25916 (Residues: 1-108; Coverage: 33%)
Gene names: Bmi-1, Bmi1, Pcgf4
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: 165 amino acids
Theoretical weight: 18.73 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9CQJ4 (Residues: 1-159; Coverage: 47%)
Gene names: DinG, Ring1b, Rnf2
Sequence domains: Zinc finger, C3HC4 type (RING finger)
Structure domains: Zinc/RING finger domain, C3HC4 (zinc finger)

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P63
Unit cell:
a: 120.046Å b: 120.046Å c: 27.096Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.181 0.179 0.213
Expression system: Escherichia coli