3znv

X-ray diffraction
1.3Å resolution

Crystal structure of the OTU domain of OTULIN at 1.3 Angstroms.

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:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-188378 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ubiquitin thioesterase otulin Chain: A
Molecule details ›
Chain: A
Length: 275 amino acids
Theoretical weight: 31.93 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

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P212121
Unit cell:
a: 43.49Å b: 72.01Å c: 94.67Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.127 0.125 0.154
Expression system: Escherichia coli BL21