6gha

X-ray diffraction
1.98Å resolution

USP15 catalytic domain structure

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:
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 Chain: A
Molecule details ›
Chain: A
Length: 365 amino acids
Theoretical weight: 41.75 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9Y4E8 (Residues: 284-468, 786-948; Coverage: 36%)
Gene names: KIAA0529, USP15
Sequence domains: Ubiquitin carboxyl-terminal hydrolase
Structure domains: Cysteine proteinases

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE MASSIF-1
Spacegroup: P21
Unit cell:
a: 48.505Å b: 62.621Å c: 62.043Å
α: 90° β: 104.97° γ: 90°
R-values:
R R work R free
0.2 0.198 0.234
Expression system: Escherichia coli