5lrw

X-ray diffraction
2Å resolution

Structure of Cezanne/OTUD7B OTU domain bound to 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)
PDBe Complex ID:
PDB-CPX-143275 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
OTU domain-containing protein 7B Chains: A, C
Molecule details ›
Chains: A, C
Length: 296 amino acids
Theoretical weight: 34.04 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q6GQQ9 (Residues: 129-266, 292-438; Coverage: 34%)
Gene names: OTUD7B, ZA20D1
Sequence domains: OTU-like cysteine protease
Ubiquitin Chains: B, D
Molecule details ›
Chains: B, D
Length: 76 amino acids
Theoretical weight: 8.55 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P0CG47 (Residues: 153-227; Coverage: 33%)
Gene name: UBB
Sequence domains: Ubiquitin family

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: R3
Unit cell:
a: 157.56Å b: 157.56Å c: 75.6Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.178 0.176 0.217
Expression system: Escherichia coli