X-ray diffraction
1.39Å resolution

Covalent fragment group deposition -- Crystal Structure of OUTB2 in complex with PCM-0103007

Source organism: Homo sapiens
Entry authors: Sethi R, Douangamath A, Resnick E, Bradley AR, Collins P, Brandao-Neto J, Talon R, Krojer T, Bountra C, Arrowsmith CH, Edwards A, London N, von Delft F

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).
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Ubiquitin thioesterase OTUB2 Chain: A
Molecule details ›
Chain: A
Length: 225 amino acids
Theoretical weight: 26.36 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
  • Canonical: Q96DC9 (Residues: 6-230; Coverage: 96%)
Gene names: C14orf137, OTB2, OTU2, OTUB2

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04-1
Spacegroup: P21
Unit cell:
a: 47.554Å b: 58.334Å c: 50.333Å
α: 90° β: 116.38° γ: 90°
R R work R free
0.149 0.147 0.198
Expression system: Escherichia coli