2ayn

X-ray diffraction
3.2Å resolution

Structure of USP14, a proteasome-associated deubiquitinating enzyme

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

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ubiquitin carboxyl-terminal hydrolase 14 Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 404 amino acids
Theoretical weight: 46.21 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P54578 (Residues: 91-494; Coverage: 82%)
Gene names: TGT, USP14
Sequence domains: Ubiquitin carboxyl-terminal hydrolase
Structure domains: Cysteine proteinases

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P212121
Unit cell:
a: 82.285Å b: 121.582Å c: 166.852Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.265 0.261 0.322
Expression system: Escherichia coli BL21(DE3)