4ksj

X-ray diffraction
1.6Å resolution

Crystal structure of the OTU domain of Gumby/Fam105B at 1.6 angstrom

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: 276 amino acids
Theoretical weight: 32.5 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q96BN8 (Residues: 79-352; Coverage: 78%)
Gene names: FAM105B, OTULIN
Sequence domains: Peptidase family C101

Ligands and Environments

2 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P212121
Unit cell:
a: 43.35Å b: 71.82Å c: 94.2Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.182 0.18 0.215
Expression system: Escherichia coli BL21(DE3)