5j7t

X-ray diffraction
3.2Å resolution

Molecular Understanding of USP7 Substrate Recognition and C-Terminal Activation

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:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-187973 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ubiquitin carboxyl-terminal hydrolase 7 Chain: A
Molecule details ›
Chain: A
Length: 671 amino acids
Theoretical weight: 77.86 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q93009 (Residues: 211-881; Coverage: 61%)
Gene names: HAUSP, USP7
Sequence domains:
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: F222
Unit cell:
a: 104.33Å b: 196.73Å c: 226.37Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.252 0.25 0.294
Expression system: Escherichia coli