PDBe 2ylm

X-ray diffraction
2.7Å resolution

Mechanism of USP7 (HAUSP) activation by its C-terminal ubiquitin-like domain (HUBL) and allosteric regulation by GMP-synthetase.

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ubiquitin carboxyl-terminal hydrolase 7 Chain: A
Molecule details ›
Chain: A
Length: 530 amino acids
Theoretical weight: 61.93 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q93009 (Residues: 560-1084; Coverage: 48%)
Gene names: HAUSP, USP7
Sequence domains: ICP0-binding domain of Ubiquitin-specific protease 7
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: P212121
Unit cell:
a: 79.98Å b: 82.31Å c: 150.63Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.192 0.191 0.216
Expression system: Escherichia coli BL21(DE3)