PDBe 4pyz

X-ray diffraction
2.84Å resolution

Crystal structure of the first two Ubl domains of Deubiquitylase USP7

Released:
Source organism: Homo sapiens
Entry authors: Walker JR, Dong A, Ong MS, Dhe-Paganon S, Kania J, Bountra C, Arrowsmith CH, Edwards AM, Tong Y, Structural Genomics Consortium (SGC)

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 Chains: A, B
Molecule details ›
Chains: A, B
Length: 273 amino acids
Theoretical weight: 31.73 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: NEW Q93009 (Residues: 537-793; Coverage: 23%)
Gene names: HAUSP, USP7
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: APS BEAMLINE 19-ID
Spacegroup: P212121
Unit cell:
a: 68.328Å b: 103.755Å c: 116.197Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.245 0.244 0.287
Expression system: Escherichia coli BL21(DE3)