PDBe 3o65

X-ray diffraction
2.7Å resolution

Crystal structure of a Josephin-ubiquitin complex: Evolutionary restraints on ataxin-3 deubiquitinating activity

Released:

Function and Biology Details

Reaction catalysed:
Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
hetero 24-mer
hetero hexamer
homo 12-mer
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ataxin-3-like protein Chains: A, C, E, G
Molecule details ›
Chains: A, C, E, G
Length: 191 amino acids
Theoretical weight: 22.27 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9H3M9 (Residues: 1-190; Coverage: 54%)
Gene names: ATX3L, ATXN3L, MJDL
Sequence domains: Josephin
Structure domains:
Ubiquitin Chains: B, D, F, H
Molecule details ›
Chains: B, D, F, H
Length: 76 amino acids
Theoretical weight: 8.55 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P0CG48 (Residues: 609-683; Coverage: 11%)
Gene name: UBC
Sequence domains: Ubiquitin family
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1

Ligands and Environments

1 bound ligand:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X6A
Spacegroup: P321
Unit cell:
a: 159.15Å b: 159.15Å c: 146.29Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.178 0.176 0.224
Expression system: Escherichia coli