4kbl

X-ray diffraction
3.3Å resolution

Structure of HHARI, a RING-IBR-RING ubiquitin ligase: autoinhibition of an Ariadne-family E3 and insights into ligation mechanism

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:
Biological process:
Cellular component:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
PDBe Complex ID:
PDB-CPX-195254 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
E3 ubiquitin-protein ligase ARIH1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 559 amino acids
Theoretical weight: 64.34 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9Y4X5 (Residues: 1-557; Coverage: 100%)
Gene names: ARI, ARIH1, HUSSY-27, MOP6, UBCH7BP
Sequence domains:
Structure domains: Four Helix Bundle (Hemerythrin (Met), subunit A)

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P41
Unit cell:
a: 147.403Å b: 147.403Å c: 86.821Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.235 0.231 0.283
Expression system: Escherichia coli