2gfo

X-ray diffraction
2Å resolution

Structure of the Catalytic Domain of Human Ubiquitin Carboxyl-terminal Hydrolase 8

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)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ubiquitin carboxyl-terminal hydrolase 8 Chain: A
Molecule details ›
Chain: A
Length: 396 amino acids
Theoretical weight: 45.65 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P40818 (Residues: 734-1110; Coverage: 34%)
Gene names: KIAA0055, UBPY, USP8
Sequence domains: Ubiquitin carboxyl-terminal hydrolase
Structure domains: Cysteine proteinases

Ligands and Environments

1 bound ligand:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-BM
Spacegroup: P61
Unit cell:
a: 67.173Å b: 67.173Å c: 194.458Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.171 0.168 0.21
Expression system: Escherichia coli BL21