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:
Sequence domains:
- Peptidase C12, ubiquitin carboxyl-terminal hydrolase
- DEUBAD domain
- Nuclear factor related to kappa-B-binding protein
- Peptidase C12, C-terminal domain
- Ubiquitinyl hydrolase-L5
- Papain-like cysteine peptidase superfamily
- Peptidase C12, ubiquitin carboxyl-terminal hydrolase superfamily
- Ubiquitinyl hydrolase, UCH37 type
Structure analysis Details
Assemblies composition:
Assembly name:
PDBe Complex ID:
PDB-CPX-180115 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ubiquitin carboxyl-terminal hydrolase isozyme L5
Molecule details ›
Nuclear factor related to kappa-B-binding protein
Molecule details ›
Chain: B
Length: 114 amino acids
Theoretical weight: 13.65 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Length: 114 amino acids
Theoretical weight: 13.65 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
Q6P4R8 (Residues: 40-153; Coverage: 9%)
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
SSRL BEAMLINE BL11-1
Spacegroup:
P4122
Expression system: Escherichia coli
