X-ray diffraction
2.25Å resolution

Structure of Bre1 RING domain

Source organism: Saccharomyces cerevisiae
Primary publication:
Structure of the yeast Bre1 RING domain.
Proteins (2015)
PMID: 25864391

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
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
E3 ubiquitin-protein ligase BRE1 Chain: A
Molecule details ›
Chain: A
Length: 69 amino acids
Theoretical weight: 7.89 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
  • Canonical: Q07457 (Residues: 632-700; Coverage: 10%)
Gene names: BRE1, YDL074C
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: APS BEAMLINE 23-ID-D
Spacegroup: P6122
Unit cell:
a: 56.765Å b: 56.765Å c: 134.858Å
α: 90° β: 90° γ: 120°
R R work R free
0.223 0.22 0.247
Expression system: Escherichia coli