X-ray diffraction
1.9Å resolution

Crystal structure of RNF146(RING-WWE)/UbcH5a/iso-ADPr complex


Function and Biology Details

Reactions catalysed:
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine
(1a) S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [(E3-independent) E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-monoubiquitinyl-[(E3-independent) ubiquitin-conjugating enzyme]-L-cysteine
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
E3 ubiquitin-protein ligase RNF146 Chains: A, C
Molecule details ›
Chains: A, C
Length: 155 amino acids
Theoretical weight: 17.86 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
  • Canonical: Q9CZW6 (Residues: 32-185; Coverage: 43%)
Gene name: Rnf146
Sequence domains:
Ubiquitin-conjugating enzyme E2 D1 Chains: B, D
Molecule details ›
Chains: B, D
Length: 154 amino acids
Theoretical weight: 17.52 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
  • Canonical: P51668 (Residues: 1-147; Coverage: 100%)
Gene names: SFT, UBC5A, UBCH5, UBCH5A, UBE2D1
Sequence domains: Ubiquitin-conjugating enzyme
Structure domains: Ubiquitin Conjugating Enzyme

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.1
Spacegroup: P21212
Unit cell:
a: 133.665Å b: 61.688Å c: 94.346Å
α: 90° β: 90° γ: 90°
R R work R free
0.188 0.186 0.222
Expression system: Escherichia coli