4ljq

X-ray diffraction
2.45Å resolution

Crystal structure of the catalytic core of E3 ligase HOIP

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
Biological process:
  • not assigned
Cellular component:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
E3 ubiquitin-protein ligase RNF31 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 223 amino acids
Theoretical weight: 25.24 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

Ligands and Environments

1 bound ligand:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: P1
Unit cell:
a: 44.209Å b: 47.767Å c: 111.145Å
α: 101.39° β: 90.12° γ: 98.92°
R-values:
R R work R free
0.248 0.206 0.243
Expression system: Escherichia coli BL21