PDBe 1yy6

X-ray diffraction
1.7Å resolution

The Crystal Structure of the N-terminal domain of HAUSP/USP7 complexed with an EBNA1 peptide

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).
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ubiquitin carboxyl-terminal hydrolase 7 Chain: A
Molecule details ›
Chain: A
Length: 155 amino acids
Theoretical weight: 18.13 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: NEW Q93009 (Residues: 54-205; Coverage: 14%)
Gene names: HAUSP, USP7
Sequence domains: MATH domain
Structure domains: Apoptosis, Tumor Necrosis Factor Receptor Associated Protein 2; Chain A
Epstein-Barr nuclear antigen 1 Chain: B
Molecule details ›
Chain: B
Length: 10 amino acids
Theoretical weight: 913 Da
Source organism: Human herpesvirus 4 strain B95-8
Expression system: Not provided
UniProt:
  • Canonical: NEW P03211 (Residues: 441-450; Coverage: 2%)
Gene names: BKRF1, EBNA1

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P41
Unit cell:
a: 70.05Å b: 70.05Å c: 45.93Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.198 0.198 0.23
Expression systems:
  • Escherichia coli BL21
  • Not provided