1wgg

Solution NMR

Solution Structure of the N-terminal Ubiquitin-like Domain of Mouse Ubiquitin Specific Protease 14 (USP14)

Released:
Source organism: Mus musculus
Entry authors: Zhao C, Tomizawa T, Koshiba S, Inoue M, Kigawa T, Yokoyama S, RIKEN Structural Genomics/Proteomics Initiative (RSGI)

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).
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-191649 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ubiquitin carboxyl-terminal hydrolase 14 Chain: A
Molecule details ›
Chain: A
Length: 96 amino acids
Theoretical weight: 10.12 KDa
Source organism: Mus musculus
Expression system: Not provided
UniProt:
  • Canonical: Q9JMA1 (Residues: 4-86; Coverage: 17%)
Gene name: Usp14
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: torsion angle dynamics
Expression system: Not provided