1w6v

Solution NMR

Solution structure of the DUSP domain of hUSP15

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 Chain: A
Molecule details ›
Chain: A
Length: 141 amino acids
Theoretical weight: 16.15 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9Y4E8 (Residues: 1-120; Coverage: 12%)
Gene names: KIAA0529, USP15
Sequence domains: DUSP domain
Structure domains: DUSP-like

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: CANDID IN CYANA AND CNS FOR WATER REFINEMENT
Expression system: Escherichia coli BL21(DE3)