4ljo

X-ray diffraction
1.56Å resolution

Structure of an active ligase (HOIP)/ubiquitin transfer complex

Released:

Function and Biology Details

Reaction catalysed:
(1a) [E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [RBR-type E3 ubiquitin transferase]-L-cysteine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [RBR-type E3 ubiquitin transferase]-S-ubiquitinyl-L-cysteine
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
E3 ubiquitin-protein ligase RNF31 Chain: A
Molecule details ›
Chain: A
Length: 223 amino acids
Theoretical weight: 25.1 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q96EP0 (Residues: 853-1072; Coverage: 21%)
Gene names: RNF31, ZIBRA
Sequence domains: E3 Ubiquitin Ligase RBR C-terminal domain
Ubiquitin Chain: B
Molecule details ›
Chain: B
Length: 76 amino acids
Theoretical weight: 8.58 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P63048 (Residues: 1-76; Coverage: 59%)
Gene names: UBA52, UBCEP2
Sequence domains: Ubiquitin family
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: P31
Unit cell:
a: 45.95Å b: 45.95Å c: 133.01Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.183 0.181 0.212
Expression system: Escherichia coli BL21