5trb

X-ray diffraction
1.8Å resolution

Crystal structure of the RNF20 RING domain

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:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-178432 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
E3 ubiquitin-protein ligase BRE1A Chain: A
Molecule details ›
Chain: A
Length: 75 amino acids
Theoretical weight: 8.72 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5VTR2 (Residues: 906-975; Coverage: 7%)
Gene names: BRE1A, RNF20
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: AUSTRALIAN SYNCHROTRON BEAMLINE MX2
Spacegroup: I212121
Unit cell:
a: 34.83Å b: 61.29Å c: 78.67Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.217 0.216 0.236
Expression system: Escherichia coli