› 3pv1

X-ray diffraction
2.6Å resolution

Crystal structure of the USP15 DUSP-UBL domains

Released:
DOI: 10.2210/pdb3pv1/pdb
PDB entry 3pv1 coloured by chain, front view.
PDB entry 3pv1 coloured by chain, side view.
PDB entry 3pv1 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural variability of the ubiquitin specific protease DUSP-UBL double domains.
Elliott PR, Liu H, Pastok MW, Grossmann GJ, Rigden DJ, Clague MJ, Urbé S, Barsukov IL
FEBS Lett 585 3385-90 (2011)
PMID: 22001210

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:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-195234 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ubiquitin carboxyl-terminal hydrolase 15 Chains: A, B
Molecule details ›
Chains: A, B
Length: 225 amino acids
Theoretical weight: 25.96 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9Y4E8 (Residues: 1-223; Coverage: 23%)
Gene names: KIAA0529, USP15
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand ACT 1 x ACT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: C2221
Unit cell:
a: 96.66Å b: 122.98Å c: 105.05Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.208 0.205 0.274
Expression system: Escherichia coli

Quick links

Citations

6 review citations

The role of UBL domains in ubiquitin-specific proteases.
Faesen et al. (2012)
5 more

2 mentions without citation

Structure and catalytic regulatory function of ubiquitin specific protease 11 N-terminal and ubiquitin-like domains.
Harper et al. (2014)
1 more