2a9u

X-ray diffraction
2.1Å resolution

Structure of the N-terminal domain of Human Ubiquitin carboxyl-terminal hydrolase 8 (USP8)

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:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domain:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-154192 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ubiquitin carboxyl-terminal hydrolase 8 Chains: A, B
Molecule details ›
Chains: A, B
Length: 144 amino acids
Theoretical weight: 17.03 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P40818 (Residues: 1-142; Coverage: 13%)
Gene names: KIAA0055, UBPY, USP8
Sequence domains: USP8 dimerisation domain
Structure domains: Phosphotransferase system, lactose/cellobiose-type IIA subunit

Ligands and Environments

No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-BM
Spacegroup: P212121
Unit cell:
a: 34.682Å b: 64.82Å c: 151.895Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.211 0.208 0.259
Expression system: Escherichia coli BL21(DE3)