PDBe 4fjv

X-ray diffraction
2.05Å resolution

Crystal Structure of Human Otubain2 and Ubiquitin Complex

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:
Biological process:
Cellular component:

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
hetero tetramer
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ubiquitin thioesterase OTUB2 Chains: A, C
Molecule details ›
Chains: A, C
Length: 237 amino acids
Theoretical weight: 27.53 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q96DC9 (Residues: 1-234; Coverage: 100%)
Gene names: C14orf137, OTB2, OTU2, OTUB2
Sequence domains: Peptidase C65 Otubain
Structure domains:
Ubiquitin Chains: B, D
Molecule details ›
Chains: B, D
Length: 86 amino acids
Theoretical weight: 9.8 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P0CG48 (Residues: 609-684; Coverage: 11%)
Gene name: UBC
Sequence domains: Ubiquitin family
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04-1
Spacegroup: P212121
Unit cell:
a: 54.063Å b: 76.825Å c: 198.847Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.209 0.206 0.267
Expression system: Escherichia coli