PDBe 3c0r

X-ray diffraction
2.32Å resolution

Structure of Ovarian Tumor (OTU) domain in complex with 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).
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 OTU1 Chains: A, C
Molecule details ›
Chains: A, C
Length: 212 amino acids
Theoretical weight: 24.15 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P43558 (Residues: 91-301; Coverage: 70%)
Gene names: OTU1, YFL044C
Sequence domains: OTU-like cysteine protease
Structure domains: Cathepsin B; Chain A
Ubiquitin Chains: B, D
Molecule details ›
Chains: B, D
Length: 75 amino acids
Theoretical weight: 8.52 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
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: APS BEAMLINE 19-ID
Spacegroup: P64
Unit cell:
a: 107.311Å b: 107.311Å c: 100.239Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.198 0.196 0.243
Expression system: Escherichia coli BL21(DE3)