PDBe 2f1x

X-ray diffraction
2.3Å resolution

Crystal structure of the TRAF-like domain of HAUSP/USP7 bound to a p53 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:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ubiquitin carboxyl-terminal hydrolase 7 Chains: A, B
Molecule details ›
Chains: A, B
Length: 161 amino acids
Theoretical weight: 18.71 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q93009 (Residues: 53-213; Coverage: 14%)
Gene names: HAUSP, USP7
Sequence domains: MATH domain
Structure domains: Apoptosis, Tumor Necrosis Factor Receptor Associated Protein 2; Chain A

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: C2
Unit cell:
a: 87.756Å b: 39.56Å c: 101.885Å
α: 90° β: 105.32° γ: 90°
R-values:
R R work R free
0.23 0.227 0.263
Expression system: Escherichia coli BL21(DE3)