1tff

X-ray diffraction
2.1Å resolution

Structure of Otubain-2

Released:
Source organism: Homo sapiens
Primary publication:
Crystal structure of human otubain 2.
EMBO Rep. 5 783-8 (2004)
PMID: 15258613

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:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ubiquitin thioesterase OTUB2 Chain: A
Molecule details ›
Chain: A
Length: 234 amino acids
Theoretical weight: 27.44 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q96DC9 (Residues: 1-234; Coverage: 100%)
Gene names: C14orf137, OTB2, OTU2, OTUB2
Sequence domains: Peptidase C65 Otubain
Structure domains:

Ligands and Environments

No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM30A, ESRF BEAMLINE ID14-4
Spacegroup: P212121
Unit cell:
a: 46.433Å b: 65.401Å c: 76.259Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.191 0.188 0.257
Expression system: Escherichia coli BL21(DE3)