6f5h

X-ray diffraction
2.16Å resolution

Crystal structure of USP7 in complex with a 4-hydroxypiperidine based inhibitor

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:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-187976 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ubiquitin carboxyl-terminal hydrolase 7 Chains: A, B
Molecule details ›
Chains: A, B
Length: 357 amino acids
Theoretical weight: 41.51 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • 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

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE MASSIF-1
Spacegroup: P21
Unit cell:
a: 74.865Å b: 67.328Å c: 80.686Å
α: 90° β: 105.06° γ: 90°
R-values:
R R work R free
0.205 0.202 0.262
Expression system: Escherichia coli