› 6wi7

X-ray diffraction
1.7Å resolution

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
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-152851 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
E3 ubiquitin-protein ligase RING2; Polycomb complex protein BMI-1 Chain: A
Molecule details ›
Chain: A
Length: 211 amino acids
Theoretical weight: 24.32 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q99496 (Residues: 10-116; Coverage: 32%)
  • Canonical: P35226 (Residues: 1-104; Coverage: 32%)
Gene names: BAP1, BMI1, DING, HIPI3, PCGF4, RING1B, RNF2, RNF51
Sequence domains: Zinc finger, C3HC4 type (RING finger)

Ligands and Environments

3 bound ligands:
Ligand ZN 4 x ZN
Ligand EPE 1 x EPE
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-G
Spacegroup: P212121
Unit cell:
a: 49.311Å b: 54.353Å c: 82.266Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.166 0.165 0.196
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

13 review citations

Super-Enhancers, Phase-Separated Condensates, and 3D Genome Organization in Cancer.
Tang et al. (2022)
12 more

1 mention without citation

Small-molecule inhibitors targeting Polycomb repressive complex 1 RING domain.
Shukla et al. (2021)