PDBe 4wph

X-ray diffraction
2.92Å resolution

Crystal structure of USP7 ubiquitin-like domains in compact conformation

Released:

Function and Biology Details

Reactions 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).
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ubiquitin carboxyl-terminal hydrolase 7 Chains: A, B
Molecule details ›
Chains: A, B
Length: 375 amino acids
Theoretical weight: 43.84 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q93009 (Residues: 514-514, 535-888; Coverage: 32%)
Gene names: HAUSP, USP7
Sequence domains: ICP0-binding domain of Ubiquitin-specific protease 7
E3 ubiquitin-protein ligase ICP0 Chains: C, D
Molecule details ›
Chains: C, D
Length: 11 amino acids
Theoretical weight: 1.32 KDa
Source organism: Human alphaherpesvirus 1 strain 17
Expression system: Not provided
UniProt:
  • Canonical: P08393 (Residues: 617-627; Coverage: 1%)
Gene names: ICP0, IE110

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: P3221
Unit cell:
a: 92.336Å b: 92.336Å c: 190.283Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.234 0.233 0.262
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided