5lrv

X-ray diffraction
2.8Å resolution

Structure of Cezanne/OTUD7B OTU domain bound to Lys11-linked diubiquitin

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 trimer (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
OTU domain-containing protein 7B Chain: A
Molecule details ›
Chain: A
Length: 318 amino acids
Theoretical weight: 36.36 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q6GQQ9 (Residues: 129-438; Coverage: 37%)
Gene names: OTUD7B, ZA20D1
Sequence domains: OTU-like cysteine protease
Ubiquitin Chain: B
Molecule details ›
Chain: B
Length: 76 amino acids
Theoretical weight: 8.55 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P0CG47 (Residues: 153-228; Coverage: 33%)
Gene name: UBB
Sequence domains: Ubiquitin family
Ubiquitin Chain: C
Molecule details ›
Chain: C
Length: 76 amino acids
Theoretical weight: 8.6 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P0CG47 (Residues: 153-227; Coverage: 33%)
Gene name: UBB
Sequence domains: Ubiquitin family

Ligands and Environments

2 bound ligands:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: P212121
Unit cell:
a: 92.03Å b: 56.52Å c: 91.75Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.209 0.207 0.244
Expression systems:
  • Escherichia coli
  • Not provided