PDBe 4m5x

X-ray diffraction
2.19Å resolution

Crystal structure of the USP7/HAUSP catalytic domain


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
Ubiquitin carboxyl-terminal hydrolase 7 Chains: A, B
Molecule details ›
Chains: A, B
Length: 355 amino acids
Theoretical weight: 41.15 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
  • Canonical: Q93009 (Residues: 207-560; Coverage: 32%)
Gene names: HAUSP, USP7
Sequence domains: Ubiquitin carboxyl-terminal hydrolase
Structure domains: ubp-family deubiquitinating enzyme superfamily

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-G
Spacegroup: P21
Unit cell:
a: 74.951Å b: 67.579Å c: 76.805Å
α: 90° β: 96.21° γ: 90°
R R work R free
0.182 0.18 0.221
Expression system: Escherichia coli