Function and Biology Details
Reactions 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).
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine
Biochemical function:
Biological process:
Cellular component:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158215 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ubiquitin thioesterase otubain-like
Molecule details ›
Chain: B
Length: 284 amino acids
Theoretical weight: 32.32 KDa
Source organism: Caenorhabditis elegans
Expression system: Escherichia coli
UniProt:
Sequence domains: Peptidase C65 Otubain
Structure domains:
Length: 284 amino acids
Theoretical weight: 32.32 KDa
Source organism: Caenorhabditis elegans
Expression system: Escherichia coli
UniProt:
- Canonical:
Q9XVR6 (Residues: 1-284; Coverage: 100%)
Sequence domains: Peptidase C65 Otubain
Structure domains:
Ubiquitin-conjugating enzyme E2 N
Molecule details ›
Chain: D
Length: 152 amino acids
Theoretical weight: 17.16 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: Ubiquitin-conjugating enzyme
Structure domains: Ubiquitin Conjugating Enzyme
Length: 152 amino acids
Theoretical weight: 17.16 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical: P61088 (Residues: 1-152; Coverage: 100%)
Sequence domains: Ubiquitin-conjugating enzyme
Structure domains: Ubiquitin Conjugating Enzyme
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
APS BEAMLINE 23-ID-D
Spacegroup:
P6122
Expression system: Escherichia coli
