PDBe 5oe7

X-ray diffraction
2.95Å resolution

Structure of OTULIN bound to the Met1-linked diubiquitin activity probe

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).
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):
Ubiquitin thioesterase otulin Chain: A
Molecule details ›
Chain: A
Length: 273 amino acids
Theoretical weight: 31.73 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q96BN8 (Residues: 80-350; Coverage: 77%)
Gene names: FAM105B, OTULIN
Sequence domains: Peptidase family C101
Ubiquitin Chain: B
Molecule details ›
Chain: B
Length: 146 amino acids
Theoretical weight: 16.49 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P0CG48 (Residues: 533-678; Coverage: 21%)
Gene name: UBC
Sequence domains: Ubiquitin family

Ligands and Environments

No bound ligands

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: R32
Unit cell:
a: 101.143Å b: 101.143Å c: 277.916Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.227 0.223 0.309
Expression systems:
  • Escherichia coli
  • Not provided