PDBe 3znz

X-ray diffraction
1.9Å resolution

Crystal structure of OTULIN OTU domain (C129A) in complex with Met1- di ubiquitin

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

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ubiquitin thioesterase otulin Chain: A
Molecule details ›
Chain: A
Length: 275 amino acids
Theoretical weight: 31.89 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q96BN8 (Residues: 80-352; Coverage: 78%)
Gene names: FAM105B, OTULIN
Sequence domains: Peptidase family C101
Ubiquitin Chain: B
Molecule details ›
Chain: B
Length: 152 amino acids
Theoretical weight: 17.14 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P0CG48 (Residues: 533-684; Coverage: 22%)
Gene name: UBC
Sequence domains: Ubiquitin family
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: R32
Unit cell:
a: 100.02Å b: 100.02Å c: 280.26Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.186 0.184 0.222
Expression system: Escherichia coli BL21