PDBe 1nb8

X-ray diffraction
2.3Å resolution

Structure of the catalytic domain of USP7 (HAUSP)

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 7 Chains: A, B
Molecule details ›
Chains: A, B
Length: 353 amino acids
Theoretical weight: 41.43 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: NEW Q93009 (Residues: 208-560; Coverage: 32%)
Gene names: HAUSP, USP7
Sequence domains: Ubiquitin carboxyl-terminal hydrolase
Structure domains: ubp-family deubiquitinating enzyme superfamily

Ligands and Environments

No bound ligands

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P21
Unit cell:
a: 75.647Å b: 68.512Å c: 76.261Å
α: 90° β: 95.36° γ: 90°
R-values:
R R work R free
0.23 0.222 0.279
Expression system: Escherichia coli