3h8h

X-ray diffraction
2Å resolution

Structure of the C-terminal domain of human RNF2/RING1B;

Released:

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
Cellular component:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
E3 ubiquitin-protein ligase RING2 Chain: A
Molecule details ›
Chain: A
Length: 112 amino acids
Theoretical weight: 12.65 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q99496 (Residues: 220-330; Coverage: 33%)
Gene names: BAP1, DING, HIPI3, RING1B, RNF2
Sequence domains: RAWUL domain RING finger- and WD40-associated ubiquitin-like
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E SUPERBRIGHT
Spacegroup: P6522
Unit cell:
a: 72.169Å b: 72.169Å c: 90.966Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.202 0.2 0.244
Expression system: Escherichia coli