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
Assembly composition:
hetero dimer (preferred)
Assembly name:
Proteasome complex (preferred)
PDBe Complex ID:
PDB-CPX-172452 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ubiquitin carboxyl-terminal hydrolase isozyme L5
Molecule details ›
Chain: A
Length: 328 amino acids
Theoretical weight: 37.53 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
Sequence domains:
Length: 328 amino acids
Theoretical weight: 37.53 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
- Canonical:
Q9WUP7 (Residues: 1-329; Coverage: 100%)
Sequence domains:
Proteasomal ubiquitin receptor ADRM1
Molecule details ›
Chain: B
Length: 99 amino acids
Theoretical weight: 10.39 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: UCH-binding domain
Length: 99 amino acids
Theoretical weight: 10.39 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical: Q16186 (Residues: 286-384; Coverage: 24%)
Sequence domains: UCH-binding domain
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
Cu FINE FOCUS
Spacegroup:
P212121
Expression system: Escherichia coli
