PDBe 5kyb

X-ray diffraction
2.2Å resolution

Crystal structure of the apo-form of USP7 catalytic domain [V302K] mutant


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: 351 amino acids
Theoretical weight: 40.62 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
  • Canonical: Q93009 (Residues: 208-554; Coverage: 32%)
Gene names: HAUSP, USP7
Sequence domains: Ubiquitin carboxyl-terminal hydrolase

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: P21
Unit cell:
a: 75.62Å b: 68.28Å c: 77.06Å
α: 90° β: 95.99° γ: 90°
R R work R free
0.216 0.213 0.276
Expression system: Escherichia coli