4a3o

X-ray diffraction
2.2Å resolution

Crystal structure of the USP15 DUSP-UBL monomer

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).
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-195233 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ubiquitin carboxyl-terminal hydrolase 15 Chains: A, B
Molecule details ›
Chains: A, B
Length: 220 amino acids
Theoretical weight: 25.51 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q9Y4E8 (Residues: 4-223; Coverage: 22%)
Gene names: KIAA0529, USP15
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: P31
Unit cell:
a: 100.419Å b: 100.419Å c: 71.704Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.202 0.201 0.229
Expression system: Escherichia coli BL21